MolNFT v1 · #30880 · protein
An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose-6- phosphate
2ACR: “An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate…”. X-ray diffraction. MolNFT v1 #30880 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2ACR
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15121
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 315 | — | P15121 |
Compared structures
- 2ACR · An anion binding site in human aldose reductase: mechanistic implications for the binding… · the same entry in another collection · chain A against A, TM-score 1.00
- P15121 · AlphaFold monomer V2.0 prediction for aldo-keto reductase family 1 member B1 (P15121) · a predicted model of the same protein · 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 P15121
- Elsewhere: RCSB PDB 2ACR · PDBe 2ACR · UniProt P15121
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