Research workbench
Larb, a CARBOXYLASE/HYDROLASE involved in synthesis of the cofactor for lactate racemase, in complex with adenosine monophosphate AMP
Analyse Larb, a CARBOXYLASE/HYDROLASE involved in synthesis of the cofactor for lactate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MJ0
- Type
- protein
- Length
- 1,213 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F9UST0
- Ligands
- AMP, MG
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 202 | — | F9UST0 |
| B | — | protein | 202 | — | F9UST0 |
| C | — | protein | 207 | — | F9UST0 |
| D | — | protein | 203 | — | F9UST0 |
| E | — | protein | 198 | — | F9UST0 |
| F | — | protein | 201 | — | F9UST0 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, C
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7MJ0 · 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 E 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 7MJ0 · PDBe 7MJ0 · UniProt F9UST0
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