MolNFT v1 · #5325 · protein

Udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase

1EEH: “Udp-N-acetylmuramoyl-L-ALANINE:D-glutamate ligase”. X-ray diffraction, 1 ligand (UMA), 4 pockets (best druggability 0.74). MolNFT v1 #5325 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1EEH
Type: protein
Length: 431 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
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 36% 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	431	36% helix, 21% strand	P14900

Ligands and binding sites

UMA · Uridine-5'-diphosphate-N-acetylmuramoyl-L-alanine · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	854	0.74	0.78	75	empty
2	114	0.38	0.75	25	UMA
3	100	0.36	0.74	16	empty
4	54	0.31	0.76	18	empty

Compared structures

1EEH · 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 0.68

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 1EEH · PDBe 1EEH · UniProt P14900

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.