MolNFT v1 · #168977 · protein
KIF14[391-735] - ADP-alfx in complex with a microtubule
6WWU: “KIF14[391-735] - ADP-alfx in complex with a microtubule”. Electron microscopy, 5 ligands (GTP, GDP, TA1). MolNFT v1 #168977 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6WWU
- Type
- protein
- Length
- 1,216 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2XVP4, A0A287AGU7, L0N7N1
- Ligands
- GTP, GDP, TA1, ADP, MG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 440 | — | Q2XVP4 |
| B | — | protein | 431 | — | A0A287AGU7 |
| K | — | protein | 345 | — | L0N7N1 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A, B
- GDP · Guanosine-5'-diphosphate · ligand · chains B
- TA1 · Taxol · ligand · chains B
- ADP · Adenosine-5'-diphosphate · ligand · chains K
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q2XVP4
- Every structure of UniProt A0A287AGU7
- Every structure of UniProt L0N7N1
- Elsewhere: RCSB PDB 6WWU · PDBe 6WWU · UniProt Q2XVP4 · UniProt A0A287AGU7 · UniProt L0N7N1
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