MolNFT v1 · #134372 · protein
Kinetic, spectral and structural characterization of the slow binding inhibitor acetopyruvate with dihydrodipicolinate synthase from escherichia COLI.
5T25: “Kinetic, spectral and structural characterization of the slow binding inhibitor acetopyruvate with…”. X-ray diffraction, 1 ligand (NA). MolNFT v1 #134372 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5T25
- Type
- protein
- Length
- 587 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B7M7I1
- Ligands
- NA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 294 | — | B7M7I1 |
| B | — | protein | 293 | — | B7M7I1 |
Ligands and binding sites
- NA · Sodium ion · metal · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5T25 · Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor… · the same entry in another collection · chain A against A, TM-score 1.00
- B7M7I1 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate synthase (B7M7I1) · a predicted model of the same protein · chain B 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 B7M7I1
- Elsewhere: RCSB PDB 5T25 · PDBe 5T25 · UniProt B7M7I1
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