Interaction between Cytochrome c iso-1 (5cib_D) and Cytochrome c peroxidase, mitochondrial (5cib_C)
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_D
Title: Cytochrome c iso-1
Source organism: Saccharomyces cerevisiae S288C
Number of residues: 108
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Chain B: 5cib_C
Title: Cytochrome c peroxidase, mitochondrial
Source organism: Saccharomyces cerevisiae S288C
Number of residues: 294
Structural properties
Hetero-dimer interface properties
Buried interface area: 471.00 Å2
Number of inter-residue contacts at the interface: 42
Number of H-bonds: 1
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_D
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 8 13 T 7.1 12.3 % 2 9 14 L 30.6 79.2 % 3 12 17 T 56.7 63.9 % 4 13 18 R 36.1 75.2 % 5 16 21 Q 37.7 43.1 % 6 17 22 C 3.9 96.1 % 7 28 33 V 29.0 29.0 % 8 70 75 N 34.7 58.3 % 9 71 76 P 1.6 16.6 % 10 72 77 K 16.2 16.9 % 11 81 86 A 42.1 60.2 % 12 82 87 F 25.2 81.7 % 13 83 88 G 36.3 47.8 % 14 84 89 G 13.9 54.2 % 15 85 90 L 4.5 23.6 % 16 86 91 K 53.9 32.9 % 17 87 92 K 31.5 26.8 % 18 90 95 D 10.1 51.4 %
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Interface residues in 5cib_C
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 31 31 R 41.7 39.8 % 2 32 32 E 5.6 4.4 % 3 34 34 D 27.0 41.1 % 4 35 35 E 16.0 12.2 % 5 38 38 N 34.1 24.7 % 6 39 39 Y 97.7 67.8 % 7 40 40 I <0.1 0.1 % 8 120 120 Q 36.4 30.9 % 9 193 193 A 40.5 90.6 % 10 194 194 A 15.1 65.4 % 11 195 195 N 3.1 13.1 % 12 196 196 N 38.5 64.4 % 13 197 197 V 37.1 91.9 % 14 199 199 T 11.1 31.8 % 15 201 201 E 3.8 13.6 % 16 229 229 Y 23.1 57.5 % 17 290 290 E 28.5 22.2 % 18 294 294 L 11.7 10.4 %
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 | 7.1 | |
2 | 9 | 14 | L | 39 | 39 | Y | 30.6 | |
3 | 12 | 17 | T | 38 | 38 | N | 34.1 | |
4 | 12 | 17 | T | 39 | 39 | Y | 22.5 | |
5 | 12 | 17 | T | 40 | 40 | I | <0.1 | |
6 | 13 | 18 | R | 39 | 39 | Y | 24.5 | |
7 | 13 | 18 | R | 196 | 196 | N | 11.6 | |
8 | 16 | 21 | Q | 193 | 193 | A | 25.8 | |
9 | 16 | 21 | Q | 195 | 195 | N | 3.1 | |
10 | 16 | 21 | Q | 229 | 229 | Y | 8.7 | |
11 | 17 | 22 | C | 193 | 193 | A | 3.9 | |
12 | 28 | 33 | V | 193 | 193 | A | 10.7 | |
13 | 28 | 33 | V | 201 | 201 | E | 3.8 | |
14 | 28 | 33 | V | 229 | 229 | Y | 14.4 | |
15 | 70 | 75 | N | 120 | 120 | Q | 7.9 | |
16 | 70 | 75 | N | 290 | 290 | E | 26.8 | H-bond |
17 | 71 | 76 | P | 120 | 120 | Q | 1.6 | |
18 | 72 | 77 | K | 120 | 120 | Q | 14.5 | |
19 | 72 | 77 | K | 290 | 290 | E | 1.7 | |
20 | 81 | 86 | A | 194 | 194 | A | 14.0 | |
21 | 81 | 86 | A | 197 | 197 | V | 17.0 | |
22 | 81 | 86 | A | 199 | 199 | T | 11.1 | |
23 | 82 | 87 | F | 120 | 120 | Q | 7.4 | |
24 | 82 | 87 | F | 194 | 194 | A | 1.1 | |
25 | 82 | 87 | F | 196 | 196 | N | 2.2 | |
26 | 82 | 87 | F | 197 | 197 | V | 14.4 | |
27 | 83 | 88 | G | 34 | 34 | D | 1.0 | |
28 | 83 | 88 | G | 120 | 120 | Q | 4.9 | |
29 | 83 | 88 | G | 196 | 196 | N | 24.6 | |
30 | 83 | 88 | G | 197 | 197 | V | 5.7 | |
31 | 84 | 89 | G | 34 | 34 | D | 13.9 | |
32 | 85 | 90 | L | 34 | 34 | D | 4.5 | |
33 | 86 | 91 | K | 31 | 31 | R | 41.0 | |
34 | 86 | 91 | K | 34 | 34 | D | 1.2 | |
35 | 86 | 91 | K | 294 | 294 | L | 11.7 | |
36 | 87 | 92 | K | 31 | 31 | R | 0.7 | |
37 | 87 | 92 | K | 32 | 32 | E | 5.6 | |
38 | 87 | 92 | K | 34 | 34 | D | 6.0 | |
39 | 87 | 92 | K | 35 | 35 | E | 16.0 | |
40 | 87 | 92 | K | 39 | 39 | Y | 3.1 | |
41 | 90 | 95 | D | 34 | 34 | D | 0.3 | |
42 | 90 | 95 | D | 39 | 39 | Y | 9.8 |
Ligands at the interaction interface
Chain | Protein | Residue no. | Ligand name | Contact area with same domain | Contact area with other domain |
---|---|---|---|---|---|
A | 5cib_D | 201 | HEM | 642.2 | 21.8 |
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: 5cib_D; 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_D: 1 TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKK 60
dssp: ---------HHHHHHH-------E-----------E------------------------
Query: 62 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 109
NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
5cib_D: 61 NVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 108
dssp: ---------------HHHH-------------HHHHHHHHHH------
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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_C; 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_C: 1 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKH 60
dssp: -----EE--------HHHHHHHHHHHHHHHHH----------HHHHHHHHHHHH---E--
Query: 128 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 187
DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ
5cib_C: 61 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 120
dssp: --E------HHH-------------HHHHH--HHHHHH-----HHHHHHHHHHHHHHH--
Query: 188 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKT 247
GPKIPWRCGRVDTPEDTTPDNGRLPDADKDA YVRTFFQRLNMNDREVVALMGAHALGKT
5cib_C: 121 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKT 180
dssp: -----E------------------------HHHHHHHH------HHHHHHHHHHHH---E
Query: 248 HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 307
HLKNSGYEGP GAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ
5cib_C: 181 HLKNSGYEGPGGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 240
dssp: --------E-----------HHHHHHHH---EEEE-----EEEE-----EE-HHHHHHHH
Query: 308 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 361
DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
5cib_C: 241 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 294
dssp: -HHHHHHHHHHHH-HHHHHHHHHHHHHHHHH--EE--------E-----HHH--