MolNFT v1 · #167304 · protein
CLPP1P2 complex from M. tuberculosis bound to adep
6VGN: “CLPP1P2 complex from M. tuberculosis bound to adep”. Electron microscopy, 1 ligand (R0M). MolNFT v1 #167304 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VGN
- Type
- protein
- Length
- 2,660 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A045HBE0, P9WPC5
- Ligands
- R0M
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | — | protein | 196 | — | A0A045HBE0 |
| H, I, J, K, L, M, N | — | protein | 178 | — | P9WPC5 |
| V, W, X, Y, Z, a, b | — | protein | 6 | — | — |
Ligands and binding sites
- R0M · (2E,4E)-hepta-2,4-dienoic acid · ligand · 7 copies · chains A, B, V, G, W, F, X, E, Y, D, Z, C, a, b
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VGN · ClpP1P2 complex from M. tuberculosis bound to ADEP · the same entry in another collection · chain Z against Z, 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 A0A045HBE0
- Every structure of UniProt P9WPC5
- Elsewhere: RCSB PDB 6VGN · PDBe 6VGN · UniProt A0A045HBE0 · UniProt P9WPC5
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