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AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q8ZIE8)

Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q8ZIE8
Type: protein
Length: 491 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
Molecule: Udp-N-acetylmuramate--L-alanine ligase
UniProt: Q8ZIE8
Pockets: 4 · best druggability 0.76

Structure

1 distinct chain · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylmuramate--L-alanine ligase	protein	491	37% helix, 24% strand	Q8ZIE8

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	1083	0.76	0.78	98	empty
2	65	0.36	0.78	18	empty
3	61	0.35	0.78	13	empty
4	54	0.31	0.76	11	empty

Compared structures

4HV4 · 2.25 ångström resolution crystal structure of udp-N-acetylmuramate--L- alanine ligase… · an experimental structure of the same protein · chain A against A, TM-score 0.93
4HV4 · 2.25 Angstrom resolution crystal structure of UDP-N-acetylmuramate--L-alanine ligase… · an experimental structure of the same protein · chain A against A, TM-score 0.93

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 Q8ZIE8
Elsewhere: UniProt Q8ZIE8 · AlphaFold DB Q8ZIE8

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