Research workbench
Human aaa+ ATPase vcp mutant - T76E, AMP-pnp bound form, conformation I
Analyse Human aaa+ ATPase vcp mutant - T76E, AMP-pnp bound form, conformation I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BPB
- Type
- protein
- Length
- 4,440 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P55072
- Ligands
- ADP, ANP
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 740 | — | P55072 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 6 copies · chains A, F, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7BPB · Human AAA+ ATPase VCP mutant - T76E, AMP-PNP bound form, Conformation I · the same entry in another collection · chain A against A, 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 P55072
- Elsewhere: RCSB PDB 7BPB · PDBe 7BPB · UniProt P55072
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