Interaction between Mitochondrial cytochrome c (2bcn_B) and Cytochrome c peroxidase, CCP (2bcn_A)
PDB and SCOP data
PDB ID: 2bcn (all binary interactions in this PDB entry)
Title: Solvent isotope effects on interfacial protein electron transfer between cytochrome c and cytochrome c peroxidase
Release date: 2006-02-28
Resolution: 1.7 Å
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Chain A: 2bcn_B
Title: Mitochondrial cytochrome c
Source organism: Saccharomyces cerevisiae
Number of residues: 108
SCOP family: a.3.1.1
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Chain B: 2bcn_A
Title: Cytochrome c peroxidase, CCP
Source organism: Saccharomyces cerevisiae
Number of residues: 296 (2 missing in structure)
SCOP family: a.93.1.1
Structural properties
Hetero-dimer interface properties
Buried interface area: 550.66 Å2
Number of inter-residue contacts at the interface: 42
Experimental structure
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Pairwise interaction
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Biological assembly
Heteromer, 3 proteins, 3 domains.
Interface structure modeling
Residues at the interaction interface
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Interface residues in 2bcn_B
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 10 10 K 25.7 26.5 % 2 13 13 T 15.1 20.8 % 3 14 14 L 21.1 94.8 % 4 17 17 T 55.9 70.7 % 5 18 18 R 67.1 77.6 % 6 21 21 Q 48.9 51.8 % 7 22 22 C 7.8 100.0 % 8 33 33 V 25.6 30.3 % 9 75 75 N 24.7 42.1 % 10 77 77 K 10.9 9.4 % 11 78 78 K 3.2 2.1 % 12 86 86 A 47.2 67.7 % 13 87 87 F 26.1 80.4 % 14 88 88 G 33.1 57.4 % 15 90 90 L 0.2 10.4 % 16 91 91 K 59.5 53.2 % 17 92 92 K 60.2 52.7 % 18 95 95 D 18.4 62.6 %
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Interface residues in 2bcn_A
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 31 33 R 70.7 52.7 % 2 32 34 E 24.4 21.3 % 3 34 36 D 48.9 71.7 % 4 35 37 E 7.5 6.2 % 5 38 40 N 33.7 23.6 % 6 39 41 Y 111.8 85.4 % 7 40 42 I 1.0 6.5 % 8 120 122 Q 35.6 30.1 % 9 193 195 A 42.7 97.7 % 10 194 196 A 16.8 84.8 % 11 195 197 N 18.9 50.7 % 12 196 198 N 30.2 54.2 % 13 197 199 V 36.1 89.0 % 14 199 201 T 14.6 40.6 % 15 201 203 E 2.5 10.8 % 16 227 229 S <0.1 0.1 % 17 229 231 Y 22.8 63.9 % 18 290 292 E 27.7 20.0 % 19 294 296 L 4.6 4.5 %
Inter-residue contacts at the interaction interface
No. | Residue no. in chain A structure | Residue no. in chain A sequence | Residue in chain A | Residue no. in chain B structure | Residue no. in chain B sequence | Residue in chain B | Contact area, Å2 | Contact type |
---|---|---|---|---|---|---|---|---|
1 | 10 | 10 | K | 35 | 37 | E | 7.5 | |
2 | 10 | 10 | K | 39 | 41 | Y | 18.1 | |
3 | 13 | 13 | T | 39 | 41 | Y | 15.1 | |
4 | 14 | 14 | L | 39 | 41 | Y | 21.1 | |
5 | 17 | 17 | T | 38 | 40 | N | 33.7 | |
6 | 17 | 17 | T | 39 | 41 | Y | 16.5 | |
7 | 17 | 17 | T | 40 | 42 | I | 1.0 | |
8 | 17 | 17 | T | 195 | 197 | N | 4.7 | |
9 | 18 | 18 | R | 34 | 36 | D | 17.7 | |
10 | 18 | 18 | R | 39 | 41 | Y | 33.4 | |
11 | 18 | 18 | R | 196 | 198 | N | 16.0 | |
12 | 21 | 21 | Q | 193 | 195 | A | 27.1 | |
13 | 21 | 21 | Q | 195 | 197 | N | 14.2 | |
14 | 21 | 21 | Q | 227 | 229 | S | <0.1 | |
15 | 21 | 21 | Q | 229 | 231 | Y | 7.5 | |
16 | 22 | 22 | C | 193 | 195 | A | 7.8 | |
17 | 33 | 33 | V | 193 | 195 | A | 7.8 | |
18 | 33 | 33 | V | 201 | 203 | E | 2.5 | |
19 | 33 | 33 | V | 229 | 231 | Y | 15.3 | |
20 | 75 | 75 | N | 290 | 292 | E | 24.4 | |
21 | 75 | 75 | N | 294 | 296 | L | 0.3 | |
22 | 77 | 77 | K | 120 | 122 | Q | 10.9 | |
23 | 78 | 78 | K | 290 | 292 | E | 3.2 | |
24 | 86 | 86 | A | 194 | 196 | A | 16.8 | |
25 | 86 | 86 | A | 197 | 199 | V | 15.8 | |
26 | 86 | 86 | A | 199 | 201 | T | 14.6 | |
27 | 87 | 87 | F | 120 | 122 | Q | 11.1 | |
28 | 87 | 87 | F | 196 | 198 | N | 3.6 | |
29 | 87 | 87 | F | 197 | 199 | V | 11.3 | |
30 | 88 | 88 | G | 120 | 122 | Q | 13.6 | |
31 | 88 | 88 | G | 196 | 198 | N | 10.6 | |
32 | 88 | 88 | G | 197 | 199 | V | 9.0 | |
33 | 90 | 90 | L | 34 | 36 | D | 0.2 | |
34 | 91 | 91 | K | 31 | 33 | R | 52.2 | |
35 | 91 | 91 | K | 34 | 36 | D | 2.8 | |
36 | 91 | 91 | K | 290 | 292 | E | 0.1 | |
37 | 91 | 91 | K | 294 | 296 | L | 4.4 | |
38 | 92 | 92 | K | 31 | 33 | R | 18.5 | |
39 | 92 | 92 | K | 32 | 34 | E | 24.4 | |
40 | 92 | 92 | K | 34 | 36 | D | 17.3 | |
41 | 95 | 95 | D | 34 | 36 | D | 10.9 | |
42 | 95 | 95 | D | 39 | 41 | Y | 7.5 |
Ligands at the interaction interface
Chain | Protein | Residue no. | Ligand name | Contact area with same domain | Contact area with other domain |
---|---|---|---|---|---|
A | 2bcn_B | 109 | HEM | 644.8 | 23.6 |
Sequence alignments
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Query protein: sp|P00044|CYC1_YEAST Cytochrome c iso-1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=CYC1 PE=1 SV=2
Result domain: 2bcn_B; Mitochondrial cytochrome c
Alignment data:
Expectation value = 1.35e-76, Score = 224 bits (569),
Identities = 99% (107/108), Positive = 99% (107/108), Gaps = 0% (0/108).
Interface alignment data:
Interface residues in alignment: 100% (18/18).
Identities = 100% (18/18), Positive = 100% (18/18), Gaps = 0% (0/18).
Query: 2 TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK 61
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK
2bcn_B: 1 TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK 60
dssp: ---------HHHHHHHHH-----E-----------E-------E----------HHHH--
Query: 62 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 109
NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKA E
2bcn_B: 61 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKASE 108
dssp: --E------HHHHH-HHHH-------------HHHHHHHHHHHHHH--
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Query protein: sp|P00431|CCPR_YEAST Cytochrome c peroxidase, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=CCP1 PE=1 SV=2
Result domain: 2bcn_A; Cytochrome c peroxidase, CCP
Alignment data:
Expectation value = 0, Score = 611 bits (1575),
Identities = 99% (292/294), Positive = 99% (292/294), Gaps = 0% (0/294).
Interface alignment data:
Interface residues in alignment: 100% (19/19).
Identities = 100% (19/19), Positive = 100% (19/19), Gaps = 0% (0/19).
Query: 68 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKH 127
TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWH SGTWDKH
2bcn_A: 3 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKH 62
dssp: -----EE--------HHHHHHHHHHHHHHHHH---HHHH---HHHHHHHHHHHH---E--
Query: 128 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 187
DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ
2bcn_A: 63 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 122
dssp: --E------HHH-HHHH--HHH---HHHHHHHHHHHHH-----HHHHHHHHHHHHHHH--
Query: 188 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKT 247
GPKIPWRCGRVDTPEDTTPDNGRLPDADKDA YVRTFFQRLNMNDREVVALMGAHALGKT
2bcn_A: 123 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKT 182
dssp: -----E--------HHH-------------HHHHHHHHH-----HHHHHHHHHHHH--EE
Query: 248 HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 307
HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ
2bcn_A: 183 HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 242
dssp: -HHHH---EE----------HHHHHHHH--EEEEE-----EEEEE----EE-HHHHHHHH
Query: 308 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 361
DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
2bcn_A: 243 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 296
dssp: -HHHHHHHHHHHH-HHHHHHHHHHHHHHHHH--EE--------E-----HHH--