Interaction between Cytochrome c iso-1 (6p42_B) and Cytochrome c peroxidase, mitochondrial (6p42_A)
PDB and SCOP data
PDB ID: 6p42 (all binary interactions in this PDB entry)
Title: Yeast cytochrome c peroxidase (W191Y:L232H) in complex with iso-1 cytochrome c
Release date: 2019-10-23
Resolution: 2.9 Å
-
Chain A: 6p42_B
Title: Cytochrome c iso-1
Source organism: Saccharomyces cerevisiae S288C
Number of residues: 103
-
Chain B: 6p42_A
Title: Cytochrome c peroxidase, mitochondrial
Source organism: Saccharomyces cerevisiae S288C
Number of residues: 294
Structural properties
Hetero-dimer interface properties
Buried interface area: 551.67 Å2
Number of inter-residue contacts at the interface: 47
Number of H-bonds: 2
Number of salt bridges: 2
Experimental structure
-
Pairwise interaction
-
Biological assembly
Heteromer, 2 proteins.
Interface structure modeling
Residues at the interaction interface
-
Interface residues in 6p42_B
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 5 5 K 16.9 18.0 % 2 8 8 T 16.0 20.5 % 3 9 9 L 19.9 98.5 % 4 12 12 T 58.2 74.6 % 5 13 13 R 60.6 71.5 % 6 16 16 Q 43.2 46.0 % 7 17 17 C 4.6 96.5 % 8 27 27 K 6.9 5.6 % 9 28 28 V 27.1 32.5 % 10 70 70 N 21.6 58.7 % 11 71 71 P 4.2 68.1 % 12 72 72 K 55.9 42.8 % 13 73 73 K 3.5 2.6 % 14 81 81 A 50.5 69.5 % 15 82 82 F 23.3 81.6 % 16 83 83 G 33.3 59.6 % 17 86 86 K 56.0 46.1 % 18 87 87 K 43.1 35.3 % 19 90 90 D 6.8 61.2 %
-
Interface residues in 6p42_A
No. Residue no. in structure Residue no. in sequence Residue name Buried ASA, Å2 Buried ASA, % 1 31 31 R 57.0 50.4 % 2 32 32 E 5.4 4.7 % 3 34 34 D 42.9 66.0 % 4 38 38 N 27.7 21.1 % 5 39 39 Y 108.9 79.2 % 6 40 40 I <0.1 0.1 % 7 120 120 Q 63.7 52.4 % 8 192 192 G 1.6 40.8 % 9 193 193 A 41.5 89.5 % 10 194 194 A 16.0 82.3 % 11 195 195 N 23.2 53.6 % 12 196 196 N 27.9 55.5 % 13 197 197 V 39.0 92.6 % 14 199 199 T 16.0 41.9 % 15 209 209 E 1.5 3.0 % 16 227 227 S 6.8 9.7 % 17 229 229 Y 15.3 46.3 % 18 290 290 E 47.3 38.3 % 19 294 294 L 9.9 8.1 %
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 | 5 | K | 39 | 39 | Y | 16.9 | |
2 | 8 | 8 | T | 39 | 39 | Y | 16.0 | |
3 | 9 | 9 | L | 39 | 39 | Y | 19.9 | |
4 | 12 | 12 | T | 38 | 38 | N | 27.7 | |
5 | 12 | 12 | T | 39 | 39 | Y | 22.5 | |
6 | 12 | 12 | T | 40 | 40 | I | <0.1 | |
7 | 12 | 12 | T | 195 | 195 | N | 8.1 | |
8 | 13 | 13 | R | 34 | 34 | D | 11.4 | |
9 | 13 | 13 | R | 39 | 39 | Y | 29.9 | |
10 | 13 | 13 | R | 196 | 196 | N | 19.4 | |
11 | 16 | 16 | Q | 192 | 192 | G | 1.6 | |
12 | 16 | 16 | Q | 193 | 193 | A | 24.9 | |
13 | 16 | 16 | Q | 194 | 194 | A | <0.1 | |
14 | 16 | 16 | Q | 195 | 195 | N | 15.2 | |
15 | 16 | 16 | Q | 229 | 229 | Y | 1.5 | |
16 | 17 | 17 | C | 193 | 193 | A | 4.6 | |
17 | 27 | 27 | K | 209 | 209 | E | 0.1 | |
18 | 27 | 27 | K | 227 | 227 | S | 6.8 | |
19 | 28 | 28 | V | 193 | 193 | A | 12.0 | |
20 | 28 | 28 | V | 209 | 209 | E | 1.3 | |
21 | 28 | 28 | V | 229 | 229 | Y | 13.8 | |
22 | 70 | 70 | N | 120 | 120 | Q | 0.6 | |
23 | 70 | 70 | N | 290 | 290 | E | 18.8 | H-bond |
24 | 70 | 70 | N | 294 | 294 | L | 2.3 | |
25 | 71 | 71 | P | 120 | 120 | Q | 4.2 | |
26 | 72 | 72 | K | 120 | 120 | Q | 31.5 | |
27 | 72 | 72 | K | 290 | 290 | E | 24.4 | H-bond, Salt bridge |
28 | 73 | 73 | K | 290 | 290 | E | 3.5 | |
29 | 81 | 81 | A | 120 | 120 | Q | 1.6 | |
30 | 81 | 81 | A | 194 | 194 | A | 16.0 | |
31 | 81 | 81 | A | 197 | 197 | V | 16.9 | |
32 | 81 | 81 | A | 199 | 199 | T | 16.0 | |
33 | 82 | 82 | F | 120 | 120 | Q | 11.3 | |
34 | 82 | 82 | F | 196 | 196 | N | 1.7 | |
35 | 82 | 82 | F | 197 | 197 | V | 10.3 | |
36 | 83 | 83 | G | 120 | 120 | Q | 14.6 | |
37 | 83 | 83 | G | 196 | 196 | N | 6.9 | |
38 | 83 | 83 | G | 197 | 197 | V | 11.8 | |
39 | 86 | 86 | K | 31 | 31 | R | 47.8 | |
40 | 86 | 86 | K | 290 | 290 | E | 0.6 | |
41 | 86 | 86 | K | 294 | 294 | L | 7.7 | |
42 | 87 | 87 | K | 31 | 31 | R | 9.2 | |
43 | 87 | 87 | K | 32 | 32 | E | 5.4 | |
44 | 87 | 87 | K | 34 | 34 | D | 25.8 | Salt bridge |
45 | 87 | 87 | K | 39 | 39 | Y | 2.7 | |
46 | 90 | 90 | D | 34 | 34 | D | 5.8 | |
47 | 90 | 90 | D | 39 | 39 | Y | 1.0 |
Ligands at the interaction interface
Chain | Protein | Residue no. | Ligand name | Contact area with same domain | Contact area with other domain |
---|---|---|---|---|---|
A | 6p42_B | 201 | HEM | 640.2 | 28.1 |
Sequence alignments
-
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: 6p42_B; Cytochrome c iso-1
Alignment data:
Expectation value = 6.80e-74, Score = 216 bits (550),
Identities = 100% (103/103), Positive = 100% (103/103), Gaps = 0% (0/103).
Interface alignment data:
Interface residues in alignment: 100% (19/19).
Identities = 100% (19/19), Positive = 100% (19/19), Gaps = 0% (0/19).
Query: 7 GSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWD 66
GSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWD
6p42_B: 1 GSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWD 60
dssp: ----HHHHHHHHH------------------------------------HHHH-------
Query: 67 ENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 109
ENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
6p42_B: 61 ENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE 103
dssp: HHHHHHHHH-HHHH--------------HHHHHHHHHHHH---
-
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: 6p42_A; Cytochrome c peroxidase, mitochondrial
Alignment data:
Expectation value = 0, Score = 606 bits (1562),
Identities = 99% (290/294), Positive = 99% (291/294), 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
6p42_A: 1 TTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKH 60
dssp: ------E--------HHHHHHHHHHHHHHHHH---HHHH---HHHHHHHHHHHHH--E--
Query: 128 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 187
DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ
6p42_A: 61 DNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQ 120
dssp: --E------HHH-HHHH--------HHHHHHHHHHHHH-----HHHHHHHHHHHHHHH--
Query: 188 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKT 247
GPKIPWRCGRVDTPEDTTPDNGRLPDADKDA YVRTFFQRLNMNDREVVALMGAHALGKT
6p42_A: 121 GPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALGKT 180
dssp: -----E------------------------HHHHHHHHHH----HHHHHHHHHHHH--EE
Query: 248 HLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQ 307
HLKNSGYEGP+GAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMM PTDYSLIQ
6p42_A: 181 HLKNSGYEGPYGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMHPTDYSLIQ 240
dssp: -HHHH---EE----------HHHHHHHH--EEEEE-----EEEEE----EE-HHHHHHHH
Query: 308 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 361
DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
6p42_A: 241 DPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL 294
dssp: -HHHHHHHHHHHH-HHHHHHHHHHHHHHHHH---E--------E----------