MolNFT v1 · #166154 · protein
Cryoem structure of human ARP2/3 complex with bound npfs
6UHC: “Cryoem structure of human ARP2/3 complex with bound npfs”. Electron microscopy, 2 ligands (ATP, MG). MolNFT v1 #166154 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UHC
- Type
- protein
- Length
- 1,940 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P61158, P61160, O15143, O15144, O15145, P59998, O15511, Q91YD9
- Ligands
- ATP, MG
Structure
electron microscopy · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 404 | — | P61158 |
| B | — | protein | 374 | — | P61160 |
| C | — | protein | 354 | — | O15143 |
| D | — | protein | 283 | — | O15144 |
| E | — | protein | 173 | — | O15145 |
| F | — | protein | 166 | — | P59998 |
| G | — | protein | 141 | — | O15511 |
| H | — | protein | 21 | — | Q91YD9 |
| I | — | protein | 24 | — | Q91YD9 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UHC · CryoEM structure of human Arp2/3 complex with bound NPFs · the same entry in another collection · chain I against I, TM-score 1.00
- O15144 · AlphaFold monomer V2.0 prediction for actin-related protein 2/3 complex subunit 2 (O15144) · a predicted model of the same protein · chain D against A, TM-score 0.99
- O15145 · AlphaFold monomer V2.0 prediction for actin-related protein 2/3 complex subunit 3 (O15145) · a predicted model of the same protein · chain E against A, TM-score 0.98
- O15143 · AlphaFold monomer V2.0 prediction for actin-related protein 2/3 complex subunit 1B… · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P61158
- Every structure of UniProt P61160
- Every structure of UniProt O15143
- Every structure of UniProt O15144
- Every structure of UniProt O15145
- Every structure of UniProt P59998
- Every structure of UniProt O15511
- Every structure of UniProt Q91YD9
- Elsewhere: RCSB PDB 6UHC · PDBe 6UHC · UniProt P61158 · UniProt P61160 · UniProt O15143 · UniProt O15144 · UniProt O15145 · UniProt P59998 · UniProt O15511 · UniProt Q91YD9
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