Interaction between Mitochondrial cytochrome c (2pcc_D) and Cytochrome c peroxidase, CCP (2pcc_C)
PDB and SCOP data
PDB ID: 2pcc (all binary interactions in this PDB entry)
Title: CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ELECTRON TRANSFER PARTNERS, CYTOCHROME C PEROXIDASE AND CYTOCHROME C
Release date: 1993-07-15
Resolution: 2.3 Å
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Chain A: 2pcc_D
Title: Mitochondrial cytochrome c
Source organism: Saccharomyces cerevisiae
Number of residues: 108
SCOP family: a.3.1.1
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Chain B: 2pcc_C
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: 498.34 Å2
Number of inter-residue contacts at the interface: 40
Number of H-bonds: 3
Number of salt bridges: 1
Experimental structure
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Pairwise interaction
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Biological assembly
Heteromer, 2 proteins, 2 domains.
Interface structure modeling
Residues at the interaction interface
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Interface residues in 2pcc_D
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 5 10 K 13.9 18.7 % 2 8 13 T 9.4 13.3 % 3 9 14 L 22.1 90.0 % 4 12 17 T 51.7 55.8 % 5 13 18 R 56.4 68.5 % 6 16 21 Q 38.3 42.4 % 7 17 22 C 6.6 100.0 % 8 28 33 V 25.5 27.5 % 9 70 75 N 20.6 45.2 % 10 72 77 K 26.3 24.2 % 11 73 78 K 16.3 10.0 % 12 81 86 A 43.0 79.9 % 13 82 87 F 21.3 75.0 % 14 83 88 G 35.4 55.6 % 15 86 91 K 49.2 40.4 % 16 87 92 K 51.8 39.4 % 17 90 95 D 10.7 46.0 %
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Interface residues in 2pcc_C
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 31 33 R 49.2 43.0 % 2 32 34 E 27.6 25.4 % 3 34 36 D 41.6 63.1 % 4 35 37 E 3.0 2.5 % 5 38 40 N 30.7 22.4 % 6 39 41 Y 98.4 72.0 % 7 120 122 Q 42.6 36.6 % 8 193 195 A 46.2 95.7 % 9 194 196 A 12.5 70.3 % 10 195 197 N 8.2 34.4 % 11 196 198 N 19.9 35.8 % 12 197 199 V 41.5 93.4 % 13 199 201 T 17.2 47.9 % 14 201 203 E 0.2 0.8 % 15 229 231 Y 14.9 39.4 % 16 290 292 E 44.7 32.3 %
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 | 5 | 10 | K | 35 | 37 | E | 2.9 | |
2 | 5 | 10 | K | 39 | 41 | Y | 11.0 | |
3 | 8 | 13 | T | 39 | 41 | Y | 9.4 | |
4 | 9 | 14 | L | 39 | 41 | Y | 22.1 | |
5 | 12 | 17 | T | 38 | 40 | N | 30.7 | |
6 | 12 | 17 | T | 39 | 41 | Y | 21.0 | |
7 | 13 | 18 | R | 34 | 36 | D | 17.2 | Salt bridge |
8 | 13 | 18 | R | 39 | 41 | Y | 32.4 | |
9 | 13 | 18 | R | 196 | 198 | N | 6.8 | |
10 | 16 | 21 | Q | 193 | 195 | A | 27.5 | H-bond |
11 | 16 | 21 | Q | 194 | 196 | A | 0.9 | |
12 | 16 | 21 | Q | 195 | 197 | N | 8.2 | |
13 | 16 | 21 | Q | 229 | 231 | Y | 1.7 | |
14 | 17 | 22 | C | 193 | 195 | A | 6.6 | |
15 | 28 | 33 | V | 193 | 195 | A | 12.1 | |
16 | 28 | 33 | V | 201 | 203 | E | 0.2 | |
17 | 28 | 33 | V | 229 | 231 | Y | 13.2 | |
18 | 70 | 75 | N | 290 | 292 | E | 20.6 | H-bond |
19 | 72 | 77 | K | 120 | 122 | Q | 17.2 | |
20 | 72 | 77 | K | 197 | 199 | V | 6.0 | |
21 | 72 | 77 | K | 199 | 201 | T | 3.2 | |
22 | 73 | 78 | K | 290 | 292 | E | 16.3 | |
23 | 81 | 86 | A | 120 | 122 | Q | 0.2 | |
24 | 81 | 86 | A | 194 | 196 | A | 11.6 | |
25 | 81 | 86 | A | 197 | 199 | V | 17.1 | |
26 | 81 | 86 | A | 199 | 201 | T | 14.1 | |
27 | 82 | 87 | F | 120 | 122 | Q | 9.6 | |
28 | 82 | 87 | F | 196 | 198 | N | 1.2 | |
29 | 82 | 87 | F | 197 | 199 | V | 10.5 | |
30 | 83 | 88 | G | 120 | 122 | Q | 15.6 | |
31 | 83 | 88 | G | 196 | 198 | N | 11.9 | |
32 | 83 | 88 | G | 197 | 199 | V | 7.9 | |
33 | 86 | 91 | K | 31 | 33 | R | 41.4 | |
34 | 86 | 91 | K | 290 | 292 | E | 7.8 | |
35 | 87 | 92 | K | 31 | 33 | R | 7.8 | |
36 | 87 | 92 | K | 32 | 34 | E | 27.6 | H-bond |
37 | 87 | 92 | K | 34 | 36 | D | 16.3 | |
38 | 87 | 92 | K | 35 | 37 | E | <0.1 | |
39 | 90 | 95 | D | 34 | 36 | D | 8.2 | |
40 | 90 | 95 | D | 39 | 41 | Y | 2.5 |
Ligands at the interaction interface
Chain | Protein | Residue no. | Ligand name | Contact area with same domain | Contact area with other domain |
---|---|---|---|---|---|
A | 2pcc_D | 104 | HEM | 631.0 | 24.8 |
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: 2pcc_D; Mitochondrial cytochrome c
Alignment data:
Expectation value = 1.54e-77, Score = 226 bits (575),
Identities = 100% (108/108), Positive = 100% (108/108), Gaps = 0% (0/108).
Interface alignment data:
Interface residues in alignment: 100% (17/17).
Identities = 100% (17/17), Positive = 100% (17/17), Gaps = 0% (0/17).
Query: 2 TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK 61
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK
2pcc_D: 1 TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK 60
dssp: ---------HHHHHHHHH-------------------------E----------HHHHH-
Query: 62 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 109
NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
2pcc_D: 61 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 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: 2pcc_C; 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% (16/16).
Identities = 100% (16/16), Positive = 100% (16/16), Gaps = 0% (0/16).
Query: 68 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKH 127
TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWH SGTWDKH
2pcc_C: 3 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKH 62
dssp: -----EE--------HHHHHHHHHHHHHHHHH---HHHH---HHHHHHHHHHHH---E--
Query: 128 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 187
DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ
2pcc_C: 63 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 122
dssp: --E------HHH-HHHH--HHH---HHHHHHHHHHHHH-----HHHHHHHHHHHHHHH--
Query: 188 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKT 247
GPKIPWRCGRVDTPEDTTPDNGRLPDADKDA YVRTFFQRLNMNDREVVALMGAHALGKT
2pcc_C: 123 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKT 182
dssp: -----E--------HHH-------------HHHHHHHHH-----HHHHHHHHHHHH---E
Query: 248 HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 307
HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ
2pcc_C: 183 HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 242
dssp: -HHHH---E-----------HHHHHHHH--EEEEE-----EEEEE----EE-HHHH----
Query: 308 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 361
DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
2pcc_C: 243 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 296
dssp: -HHHHHHHHHHHH-HHHHHHHHHHHHHHHHH--EE--------E-----HHH--