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Crystal structure of udp-N-acetylmuramate-alanine ligase murc (TM0231) from thermotoga maritima at 2.3 a resolution

Analyse Crystal structure of udp-N-acetylmuramate-alanine ligase murc (TM0231) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J6U
Type: protein
Length: 430 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-N-acetylmuramate-alanine ligase murc
EC: 6.3.2.8
UniProt: Q9WY73
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylmuramate-alanine ligase murc (EC 6.3.2.8)	protein	430	37% helix, 24% strand	Q9WY73

Pockets

2 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	1010	0.80	0.82	97	empty
2	129	0.46	0.78	29	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

1J6U · Crystal structure of UDP-N-acetylmuramate-alanine ligase MurC (TM0231) from Thermotoga… · the same entry in another collection · chain A against A, TM-score 1.00
Q9WY73 · AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q9WY73) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9WY73
Elsewhere: RCSB PDB 1J6U · PDBe 1J6U · UniProt Q9WY73

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