MolNFT v1 · #167306 · protein
CLPP1P2 complex from M. tuberculosis with glf-cmk bound to CLPP1
6VGQ: “CLPP1P2 complex from M. tuberculosis with glf-cmk bound to CLPP1”. Electron microscopy, 1 ligand (0QE). MolNFT v1 #167306 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VGQ
- Type
- protein
- Length
- 2,527 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P9WPC5, A0A045HBE0
- Ligands
- 0QE
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| N, H, I, J, K, L, M | — | protein | 178 | — | P9WPC5 |
| A, B, C, D, E, F, G | — | protein | 180 | — | A0A045HBE0 |
| U, O, P, Q, R, S, T | — | protein | 3 | — | — |
Ligands and binding sites
- 0QE · Chloromethane · ion · 7 copies · chains N, U, H, O, I, P, J, Q, K, R, L, S, M, T
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VGQ · ClpP1P2 complex from M. tuberculosis with GLF-CMK bound to ClpP1 · the same entry in another collection · chain C against C, 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 P9WPC5
- Every structure of UniProt A0A045HBE0
- Elsewhere: RCSB PDB 6VGQ · PDBe 6VGQ · UniProt P9WPC5 · UniProt A0A045HBE0
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