Research workbench
Electron transfer complex of cytochrome C and cytochrome C oxidase at 2.0 ångström resolution
Analyse Electron transfer complex of cytochrome C and cytochrome C oxidase at 2.0… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IY5
- Type
- protein
- Length
- 3,766 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C oxidase subunit 1; Cytochrome C oxidase subunit 2; Cytochrome C oxidase…
- EC
- 1.9.3.1
- UniProt
- P00396, P68530, P00415, P00423, P00426, P00428, P07471, P00429, P04038, P07470, P13183, P00430, P10175, P00004
- Ligands
- UNL, CHD, PGV, TGL, HEA, CDL, ACE, CUA, PEK, PSC, HEC, NA, CU, MG, ZN, PER
- Pockets
- 20 · best druggability 0.91
Structure
x-ray diffraction · 14 distinct chains · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, N | Cytochrome C oxidase subunit 1 (EC 1.9.3.1) | protein | 514 | 72% helix, 1% strand | P00396 |
| B, O | Cytochrome C oxidase subunit 2 | protein | 227 | 35% helix, 26% strand | P68530 |
| C, P | Cytochrome C oxidase subunit 3 | protein | 259 | 76% helix, 0% strand | P00415 |
| D, Q | Cytochrome C oxidase subunit 4 isoform 1, mitochondrial | protein | 144 | 52% helix, 3% strand | P00423 |
| E, R | Cytochrome C oxidase subunit 5A, mitochondrial | protein | 105 | 64% helix, 1% strand | P00426 |
| F, S | Cytochrome C oxidase subunit 5B, mitochondrial | protein | 98 | 15% helix, 27% strand | P00428 |
| G, T | Cytochrome C oxidase subunit 6A2, mitochondrial | protein | 84 | 29% helix, 2% strand | P07471 |
| H, U | Cytochrome C oxidase subunit 6B1 | protein | 79 | 58% helix, 1% strand | P00429 |
| I, V | Cytochrome C oxidase subunit 6C | protein | 73 | 67% helix, 1% strand | P04038 |
| J, W | Cytochrome C oxidase subunit 7A1, mitochondrial | protein | 58 | 69% helix, 0% strand | P07470 |
| K, X | Cytochrome C oxidase subunit 7B, mitochondrial | protein | 49 | 53% helix, 0% strand | P13183 |
| L, Y | Cytochrome C oxidase subunit 7C, mitochondrial | protein | 46 | 63% helix, 0% strand | P00430 |
| M, Z | Cytochrome C oxidase subunit 8B, mitochondrial | protein | 43 | 67% helix, 2% strand | P10175 |
| 1, 2 | Cytochrome C | protein | 104 | 40% helix, 2% strand | P00004 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · 15 copies · chains C, G, A, J, L, M, N, O, Y, Q, X, P, T, W, B, Z
- CHD · Cholic acid · ligand · 8 copies · chains A, C, P, J, F, G, N, O, W, B, T
- PGV · (1R)-2-{[{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy) phosphoryl]oxy}-1-[(palmitoyloxy)methyl]ethyl (11E)-octadec-11-enoate · ligand · 7 copies · chains A, D, K, M, C, F, H, P, T, N, S, G, U
- TGL · Tristearoylglycerol · ligand · 5 copies · chains A, B, I, D, K, L, N, O, V, Q
- HEA · Heme-A · ligand · 4 copies · chains A, B, N, O
- CDL · Cardiolipin · ligand · 4 copies · chains C, J, G, N, O, P, W, A, B, T
- ACE · Acetyl group · ligand · 2 copies · chains 1, 2
- CUA · Dinuclear copper ion · ligand · 2 copies · chains B, O
- PEK · (1S)-2-{[(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(stearoyloxy)methyl]ethyl (5E,8E,11E,14E)-icosa-5,8, 11,14-tetraenoate · ligand · 2 copies · chains A, C, G, N, P, T
- PSC · (7R,17E,20E)-4-hydroxy-N,N,N-trimethyl-9-oxo-7-[(palmitoyloxy)methyl]-3,5,8-trioxa-4-phosphahexacosa-17,20-dien-1-aminium 4-oxide · ligand · 2 copies · chains A, B, E, I, N, O, R, V
- HEC · Heme C · ligand · 2 copies · chains 1, 2
- NA · Sodium ion · metal · 4 copies · chains A, C, N, P
- CU · Copper (II) ion · metal · 2 copies · chains A, N
- MG · Magnesium ion · metal · 2 copies · chains A, B, N, O
- ZN · Zinc ion · metal · 2 copies · chains F, S
- PER · Peroxide ion · ion · 2 copies · chains A, N
- EDO · 1,2-ethanediol · additive · 9 copies · chains A, B, C, H, E, F, G, D, I, N, Z, P, S
- DMU · Decyl-beta-D-maltopyranoside · additive · 2 copies · chains A, D, L, M, N, Q, Y, Z
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1113 | 0.91 | 0.93 | 133 | HEA, PER, UNL |
| 2 | 1195 | 0.91 | 0.92 | 136 | HEA, PER |
| 3 | 990 | 0.86 | 0.86 | 80 | PGV |
| 4 | 722 | 0.85 | 0.88 | 84 | PGV |
| 5 | 986 | 0.84 | 0.85 | 105 | EDO |
Interfaces
86 interfaces between chains.
- N–O · 3638 Ų buried · 44 hydrogen bonds · protein-protein
- A–B · 3618 Ų buried · 39 hydrogen bonds · protein-protein
- A–C · 2632 Ų buried · 17 hydrogen bonds · protein-protein
- N–P · 2629 Ų buried · 16 hydrogen bonds · protein-protein
- A–L · 1781 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 4 cofactor, 4 disulfide, 2 covalent (heme c attachment, disulfide, formylation, covalent ligand, acetylation, phosphorylation).
Compared structures
- 5IY5 · Electron transfer complex of cytochrome c and cytochrome c oxidase at 2.0 angstrom… · the same entry in another collection · chain J against J, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P00396
- Every structure of UniProt P68530
- Every structure of UniProt P00415
- Every structure of UniProt P00423
- Every structure of UniProt P00426
- Every structure of UniProt P00428
- Every structure of UniProt P07471
- Every structure of UniProt P00429
- Every structure of UniProt P04038
- Every structure of UniProt P07470
- Every structure of UniProt P13183
- Every structure of UniProt P00430
- Every structure of UniProt P10175
- Every structure of UniProt P00004
- Elsewhere: RCSB PDB 5IY5 · PDBe 5IY5 · UniProt P00396 · UniProt P68530 · UniProt P00415 · UniProt P00423 · UniProt P00426 · UniProt P00428 · UniProt P07471 · UniProt P00429 · UniProt P04038 · UniProt P07470 · UniProt P13183 · UniProt P00430 · UniProt P10175 · UniProt P00004
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