Research workbench
Structure of human aldose reductase mutant L300A with a citrate molecule bound in the anion binding pocket
Analyse Structure of human aldose reductase mutant L300A with a citrate molecule bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T5G
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldo-keto reductase family 1 member B1
- EC
- 1.1.1.300, 1.1.1.372, 1.1.1.54, 1.1.1.21
- UniProt
- P15121
- Ligands
- NAP
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldo-keto reductase family 1 member B1 (EC 1.1.1.300, 1.1.1.372, 1.1.1.54, 1.1.1.21) | protein | 316 | 39% helix, 15% strand | P15121 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- CIT · Citric acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.71 | 0.83 | 54 | CIT, NAP |
| 2 | 69 | 0.44 | 0.82 | 21 | empty |
Compared structures
- 6T5G · Structure of Human Aldose Reductase Mutant L300A with a Citrate Molecule Bound in the… · 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 0.99
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 6T5G · PDBe 6T5G · UniProt P15121
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