MolNFT v1 · #178982 · protein
Plant mitochondrial complex sc III2+IV from vigna radiata
7JRP: “Plant mitochondrial complex sc III2+IV from vigna radiata”. Electron microscopy, 10 ligands (3PE, CDL, PC1). MolNFT v1 #178982 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7JRP
- Type
- protein
- Length
- 5,472 residues
- Chains
- 30
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1S3TWG4, A0A1S3VF71, A0A1S3W199, A0A1S3TB49, A0A1S3U9J1, A0A1S3U9S5, A0A1S3VHC0, A0A1S3TQD2, A0A1S3TZB2, A0A1S3TNX9, A0A1S3U1E4, A0A1S3UMA0, A0A1S3VV60, A0A1S3V319, A0A1S3TUX2, A0A1S3V7C2
- Ligands
- 3PE, CDL, PC1, HEM, HEC, HEA, CUA, ZN, CU, MG
Structure
electron microscopy · 25 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, M | — | protein | 487 | — | A0A1S3TWG4 |
| B | — | protein | 457 | — | A0A1S3VF71 |
| C, O | — | protein | 388 | — | — |
| D, P | — | protein | 244 | — | A0A1S3W199 |
| E, Q | — | protein | 74 | — | A0A1S3TB49 |
| F | — | protein | 116 | — | A0A1S3U9J1 |
| G, S | — | protein | 70 | — | A0A1S3U9S5 |
| H | — | protein | 65 | — | A0A1S3VHC0 |
| J | — | protein | 60 | — | A0A1S3TQD2 |
| K | — | protein | 31 | — | — |
| N | — | protein | 455 | — | A0A1S3VF71 |
| R | — | protein | 115 | — | A0A1S3U9J1 |
| T | — | protein | 64 | — | A0A1S3VHC0 |
| V | — | protein | 59 | — | A0A1S3TQD2 |
| W | — | protein | 32 | — | — |
| a | — | protein | 524 | — | — |
| b | — | protein | 239 | — | A0A1S3TZB2 |
| c | — | protein | 265 | — | — |
| d | — | protein | 76 | — | A0A1S3TNX9 |
| e | — | protein | 94 | — | A0A1S3U1E4 |
| f | — | protein | 59 | — | A0A1S3UMA0 |
| g | — | protein | 74 | — | A0A1S3VV60 |
| h | — | protein | 49 | — | A0A1S3V319 |
| i | — | protein | 65 | — | A0A1S3TUX2 |
| j | — | protein | 47 | — | A0A1S3V7C2 |
Ligands and binding sites
- 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 29 copies · chains C, O, R, F, G, D, E, K, S, P, a, c, d, j, f, b, h, i
- CDL · Cardiolipin · ligand · 9 copies · chains A, C, K, D, E, F, G, M, O, W, P, Q, S, R, a, j
- PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 5 copies · chains A, E, J, K, M, Q, V, P, S, a, c, i, j
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains C, O
- HEC · Heme C · ligand · 2 copies · chains D, P
- HEA · Heme-A · ligand · 2 copies · chains a, b
- CUA · Dinuclear copper ion · ligand · chains b
- ZN · Zinc ion · metal · 3 copies · chains A, M, e
- CU · Copper (II) ion · metal · chains a
- MG · Magnesium ion · metal · chains a, b
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JRP · Plant Mitochondrial complex SC III2+IV from Vigna radiata · the same entry in another collection · chain A against A, 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 A0A1S3TWG4
- Every structure of UniProt A0A1S3VF71
- Every structure of UniProt A0A1S3W199
- Every structure of UniProt A0A1S3TB49
- Every structure of UniProt A0A1S3U9J1
- Every structure of UniProt A0A1S3U9S5
- Every structure of UniProt A0A1S3VHC0
- Every structure of UniProt A0A1S3TQD2
- Every structure of UniProt A0A1S3TZB2
- Every structure of UniProt A0A1S3TNX9
- Every structure of UniProt A0A1S3U1E4
- Every structure of UniProt A0A1S3UMA0
- Every structure of UniProt A0A1S3VV60
- Every structure of UniProt A0A1S3V319
- Every structure of UniProt A0A1S3TUX2
- Every structure of UniProt A0A1S3V7C2
- Elsewhere: RCSB PDB 7JRP · PDBe 7JRP · UniProt A0A1S3TWG4 · UniProt A0A1S3VF71 · UniProt A0A1S3W199 · UniProt A0A1S3TB49 · UniProt A0A1S3U9J1 · UniProt A0A1S3U9S5 · UniProt A0A1S3VHC0 · UniProt A0A1S3TQD2 · UniProt A0A1S3TZB2 · UniProt A0A1S3TNX9 · UniProt A0A1S3U1E4 · UniProt A0A1S3UMA0 · UniProt A0A1S3VV60 · UniProt A0A1S3V319 · UniProt A0A1S3TUX2 · UniProt A0A1S3V7C2
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