MolNFT v1 · #23774 · protein
Udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase
1UAG · Udp-N-acetylmuramoyl-L-ALANINE/:D-glutamate ligase: “Udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase”. X-ray diffraction, 2 ligands (UMA, SO4), 3 pockets (best druggability 0.75). MolNFT v1 #23774 on GenesisL1: 3D structure…
- PDB
- 1UAG
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylmuramoyl-L-ALANINE/:D-glutamate ligase
- EC
- 6.3.2.9
- UniProt
- P14900
- Ligands
- UMA, SO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoyl-L-ALANINE/:D-glutamate ligase (EC 6.3.2.9) | protein | 428 | 37% helix, 21% strand | P14900 |
Ligands and binding sites
- UMA · Uridine-5'-diphosphate-N-acetylmuramoyl-L-alanine · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 873 | 0.75 | 0.79 | 82 | SO4, UMA |
| 2 | 212 | 0.52 | 0.77 | 24 | empty |
| 3 | 55 | 0.29 | 0.75 | 10 | empty |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, carboxylation).
Compared structures
- 1UAG · 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 1UAG · PDBe 1UAG · UniProt P14900
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