MolNFT v1 · #1254 · protein
Triosephosphate isomerase of vibrio marinus complexed with 2-phosphoglycolate
1AW1: “Triosephosphate isomerase of vibrio marinus complexed with 2-phosphoglycolate”. X-ray diffraction. MolNFT v1 #1254 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1AW1
- Type
- protein
- Length
- 2,036 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50921
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | — | protein | 255 | — | P50921 |
| B, E, H, K | — | protein | 254 | — | P50921 |
Compared structures
- 1AW1 · Triosephosphate isomerase of vibrio marinus complexed with 2-phosphoglycolate · the same entry in another collection · chain E against E, TM-score 1.00
- P50921 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P50921) · 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 P50921
- Elsewhere: RCSB PDB 1AW1 · PDBe 1AW1 · UniProt P50921
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