MolNFT v1 · #182174 · protein
Larb, a CARBOXYLASE/HYDROLASE involved in synthesis of the cofactor for lactate racemase, in complex with zn
7MJ2: “Larb, a CARBOXYLASE/HYDROLASE involved in synthesis of the cofactor for lactate racemase, in complex with zn”. X-ray diffraction, 2 ligands (MG, ZN). MolNFT v1 #182174 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7MJ2
- Type
- protein
- Length
- 1,217 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F9UST0
- Ligands
- MG, ZN
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 208 | — | F9UST0 |
| B, C, E, F | — | protein | 201 | — | F9UST0 |
| D | — | protein | 205 | — | F9UST0 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A, C, D
- ZN · Zinc ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7MJ2 · LarB, a carboxylase/hydrolase involved in synthesis of the cofactor for lactate racemase… · the same entry in another collection · chain F against F, TM-score 1.00
- F9UST0 · AlphaFold monomer V2.0 prediction for pyridinium-3,5-biscarboxylic acid mononucleotide… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 F9UST0
- Elsewhere: RCSB PDB 7MJ2 · PDBe 7MJ2 · UniProt F9UST0
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