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AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoyl-tripeptide --D-alanyl-D-alanine ligase (P11880)

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

Accession: P11880
Type: protein
Length: 452 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x0DCCBa59b2b48397411CAC3f11C2EbBaBBa4e79C
Molecule: Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
UniProt: P11880
Pockets: 3 · best druggability 0.72

Structure

1 distinct chain · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase	protein	452	39% helix, 24% strand	P11880

Pockets

3 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	500	0.72	0.82	73	empty
2	94	0.35	0.75	25	empty
3	72	0.32	0.74	17	empty

Compared structures

1GG4 · Crystal structure of escherichia COLI udpmurnac-tripeptide D-alanyl-D- alanine-adding… · an experimental structure of the same protein · chain A against A, TM-score 0.80
1GG4 · Crystal structure of escherichia COLI udpmurnac-tripeptide D-alanyl-D-alanine-adding… · an experimental structure of the same protein · chain A against A, TM-score 0.80

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 P11880
Elsewhere: UniProt P11880 · AlphaFold DB P11880

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