MolNFT v1 · #50976 · protein
Udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase
2UAG · Protein (udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase): “Udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase”. X-ray diffraction, 3 ligands (UMA, ADP, MG), 2 pockets (best druggability 0.79). MolNFT v1 #50976 on GenesisL1: 3D…
- PDB
- 2UAG
- Type
- protein
- Length
- 429 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase)
- EC
- 6.3.2.9
- UniProt
- P14900
- Ligands
- UMA, ADP, MG
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase) (EC 6.3.2.9) | protein | 429 | 35% helix, 22% strand | P14900 |
Ligands and binding sites
- UMA · Uridine-5'-diphosphate-N-acetylmuramoyl-L-alanine · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 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 | 1159 | 0.79 | 0.81 | 104 | MG, UMA, ADP |
| 2 | 72 | 0.34 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 2UAG · Udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase · the same entry in another collection · chain A against A, TM-score 1.00
- P14900 · AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P14900
- Elsewhere: RCSB PDB 2UAG · PDBe 2UAG · UniProt P14900
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