MolNFT v1 · #176496 · protein
Lp major histidine acid phosphatase mutant D281A/5'-AMP
7DOQ: “Lp major histidine acid phosphatase mutant D281A/5'-AMP”. X-ray diffraction, 1 ligand (PO4). MolNFT v1 #176496 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7DOQ
- Type
- protein
- Length
- 1,328 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2S6F805
- Ligands
- PO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 335 | — | A0A2S6F805 |
| B, C, D | — | protein | 331 | — | A0A2S6F805 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 7 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7DOQ · Lp major histidine acid phosphatase mutant D281A/5'-AMP · 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 A0A2S6F805
- Elsewhere: RCSB PDB 7DOQ · PDBe 7DOQ · UniProt A0A2S6F805
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