MolNFT v1 · #167273 · protein
Clpxp from neisseria meningitidis - conformation a
6VFS: “Clpxp from neisseria meningitidis - conformation a”. Electron microscopy, 3 ligands (ATP, ADP, MG). MolNFT v1 #167273 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VFS
- Type
- protein
- Length
- 4,583 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0Y4ZJG4, A0A0Y5K536
- Ligands
- ATP, ADP, MG
Structure
electron microscopy · 12 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 334 | — | A0A0Y4ZJG4 |
| A | — | protein | 295 | — | A0A0Y4ZJG4 |
| F | — | protein | 302 | — | A0A0Y4ZJG4 |
| C | — | protein | 330 | — | A0A0Y4ZJG4 |
| B | — | protein | 318 | — | A0A0Y4ZJG4 |
| D | — | protein | 326 | — | A0A0Y4ZJG4 |
| G | — | protein | 7 | — | — |
| L, O, P, Q, R, S, T, U, J, N | — | protein | 191 | — | A0A0Y5K536 |
| H | — | protein | 190 | — | A0A0Y5K536 |
| I | — | protein | 192 | — | A0A0Y5K536 |
| K | — | protein | 193 | — | A0A0Y5K536 |
| M | — | protein | 186 | — | A0A0Y5K536 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains E, F, C, D, B
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, F
- MG · Magnesium ion · metal · 4 copies · chains E, F, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VFS · ClpXP from Neisseria meningitidis - Conformation A · the same entry in another collection · chain E against E, 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 A0A0Y4ZJG4
- Every structure of UniProt A0A0Y5K536
- Elsewhere: RCSB PDB 6VFS · PDBe 6VFS · UniProt A0A0Y4ZJG4 · UniProt A0A0Y5K536
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