Interaction between Cytochrome c iso-1 (5cib_B) and Cytochrome c peroxidase, mitochondrial (5cib_A)
PDB and SCOP data
PDB ID: 5cib (all binary interactions in this PDB entry)
Title: Complex of yeast cytochrome c peroxidase (W191G) bound to 2,4-dimethylaniline with iso-1 cytochrome c
Release date: 2016-08-03
Resolution: 3.0 Å
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Chain A: 5cib_B
Title: Cytochrome c iso-1
Source organism: Saccharomyces cerevisiae S288C
Number of residues: 108
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Chain B: 5cib_A
Title: Cytochrome c peroxidase, mitochondrial
Source organism: Saccharomyces cerevisiae S288C
Number of residues: 294
Structural properties
Hetero-dimer interface properties
Buried interface area: 519.42 Å2
Number of inter-residue contacts at the interface: 41
Number of salt bridges: 3
Experimental structure
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Pairwise interaction
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Biological assembly
Heteromer, 4 proteins.
Interface structure modeling
Residues at the interaction interface
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Interface residues in 5cib_B
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 8 13 T 10.7 16.1 % 2 9 14 L 25.4 80.7 % 3 11 16 K 8.4 6.8 % 4 12 17 T 54.1 75.1 % 5 13 18 R 60.9 73.7 % 6 16 21 Q 29.9 32.9 % 7 17 22 C 7.4 100.0 % 8 28 33 V 26.4 29.0 % 9 70 75 N 20.9 43.8 % 10 72 77 K 56.2 40.8 % 11 73 78 K 7.6 4.8 % 12 81 86 A 45.2 63.5 % 13 82 87 F 23.9 75.0 % 14 83 88 G 32.1 53.8 % 15 85 90 L <0.1 0.0 % 16 86 91 K 48.6 40.0 % 17 87 92 K 49.9 48.0 % 18 90 95 D 12.0 32.8 %
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Interface residues in 5cib_A
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 31 31 R 58.3 50.9 % 2 32 32 E 17.5 16.7 % 3 34 34 D 42.6 64.6 % 4 35 35 E 0.7 0.6 % 5 38 38 N 36.4 27.5 % 6 39 39 Y 88.8 64.5 % 7 40 40 I 7.6 27.0 % 8 120 120 Q 55.4 48.7 % 9 193 193 A 45.1 86.8 % 10 194 194 A 15.9 75.2 % 11 195 195 N 2.3 14.0 % 12 196 196 N 25.5 47.0 % 13 197 197 V 37.1 91.3 % 14 199 199 T 11.9 33.1 % 15 201 201 E 0.8 2.8 % 16 229 229 Y 13.3 36.7 % 17 290 290 E 53.1 41.3 % 18 294 294 L 7.1 6.6 %
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 | 8 | 13 | T | 39 | 39 | Y | 10.7 | |
2 | 9 | 14 | L | 39 | 39 | Y | 25.4 | |
3 | 11 | 16 | K | 38 | 38 | N | 8.4 | |
4 | 12 | 17 | T | 38 | 38 | N | 28.0 | |
5 | 12 | 17 | T | 39 | 39 | Y | 20.7 | |
6 | 12 | 17 | T | 40 | 40 | I | 5.4 | |
7 | 13 | 18 | R | 34 | 34 | D | 15.8 | Salt bridge |
8 | 13 | 18 | R | 39 | 39 | Y | 30.0 | |
9 | 13 | 18 | R | 196 | 196 | N | 15.1 | |
10 | 16 | 21 | Q | 40 | 40 | I | 2.3 | |
11 | 16 | 21 | Q | 193 | 193 | A | 24.8 | |
12 | 16 | 21 | Q | 195 | 195 | N | 2.3 | |
13 | 16 | 21 | Q | 229 | 229 | Y | 0.4 | |
14 | 17 | 22 | C | 193 | 193 | A | 7.4 | |
15 | 28 | 33 | V | 193 | 193 | A | 12.8 | |
16 | 28 | 33 | V | 201 | 201 | E | 0.8 | |
17 | 28 | 33 | V | 229 | 229 | Y | 12.8 | |
18 | 70 | 75 | N | 290 | 290 | E | 18.9 | |
19 | 70 | 75 | N | 294 | 294 | L | 2.0 | |
20 | 72 | 77 | K | 120 | 120 | Q | 29.5 | |
21 | 72 | 77 | K | 290 | 290 | E | 26.6 | Salt bridge |
22 | 73 | 78 | K | 290 | 290 | E | 7.6 | |
23 | 81 | 86 | A | 120 | 120 | Q | 0.4 | |
24 | 81 | 86 | A | 194 | 194 | A | 15.9 | |
25 | 81 | 86 | A | 197 | 197 | V | 16.9 | |
26 | 81 | 86 | A | 199 | 199 | T | 11.9 | |
27 | 82 | 87 | F | 120 | 120 | Q | 11.0 | |
28 | 82 | 87 | F | 196 | 196 | N | 3.6 | |
29 | 82 | 87 | F | 197 | 197 | V | 9.3 | |
30 | 83 | 88 | G | 120 | 120 | Q | 14.5 | |
31 | 83 | 88 | G | 196 | 196 | N | 6.8 | |
32 | 83 | 88 | G | 197 | 197 | V | 10.9 | |
33 | 85 | 90 | L | 34 | 34 | D | <0.1 | |
34 | 86 | 91 | K | 31 | 31 | R | 43.5 | |
35 | 86 | 91 | K | 294 | 294 | L | 5.1 | |
36 | 87 | 92 | K | 31 | 31 | R | 14.8 | |
37 | 87 | 92 | K | 32 | 32 | E | 17.5 | |
38 | 87 | 92 | K | 34 | 34 | D | 16.9 | Salt bridge |
39 | 87 | 92 | K | 35 | 35 | E | 0.7 | |
40 | 90 | 95 | D | 34 | 34 | D | 9.9 | |
41 | 90 | 95 | D | 39 | 39 | Y | 2.1 |
Ligands at the interaction interface
Chain | Protein | Residue no. | Ligand name | Contact area with same domain | Contact area with other domain |
---|---|---|---|---|---|
A | 5cib_B | 201 | HEM | 632.2 | 24.0 |
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: 5cib_B; Cytochrome c iso-1
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% (18/18).
Identities = 100% (18/18), Positive = 100% (18/18), Gaps = 0% (0/18).
Query: 2 TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK 61
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK
5cib_B: 1 TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK 60
dssp: ------------HHHHHH-------------------------E----------HHHHH-
Query: 62 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 109
NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
5cib_B: 61 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 108
dssp: --E----HHHHHHH-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: 5cib_A; Cytochrome c peroxidase, mitochondrial
Alignment data:
Expectation value = 0, Score = 607 bits (1564),
Identities = 99% (291/294), Positive = 99% (291/294), Gaps = 0% (0/294).
Interface alignment data:
Interface residues in alignment: 100% (18/18).
Identities = 100% (18/18), Positive = 100% (18/18), Gaps = 0% (0/18).
Query: 68 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKH 127
TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWH SGTWDKH
5cib_A: 1 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKH 60
dssp: ------E--------HHHHHHHHHHHHHHHHH---HHHH---HHHHHHHHHHHH---E--
Query: 128 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 187
DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ
5cib_A: 61 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 120
dssp: --E----------------------HHHHHHHHHHHHH-----HHHHHHHHHHHHHHH--
Query: 188 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKT 247
GPKIPWRCGRVDTPEDTTPDNGRLPDADKDA YVRTFFQRLNMNDREVVALMGAHALGKT
5cib_A: 121 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKT 180
dssp: -----E--------HHH-------------HHHHHHHHH-----HHHHHHHHHHHH---E
Query: 248 HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 307
HLKNSGYEGP GAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ
5cib_A: 181 HLKNSGYEGPGGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 240
dssp: --------E-----------HHHHHHHH--EEEEE-----EEEEE----EE-HHHHHHHH
Query: 308 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 361
DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
5cib_A: 241 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 294
dssp: -HHHHHHHHHHHH-HHHHHHHHHHHHHHHHH---E--------E----------