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Crystal structure II of murf from acinetobacter baumannii

Analyse Crystal structure II of murf from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QDI
Type: protein
Length: 457 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
EC: 6.3.2.10
UniProt: B7GVN5
Ligands: ATP, UDP, MG
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase (EC 6.3.2.10)	protein	457	37% helix, 23% strand	B7GVN5

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
UDP · Uridine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

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	724	0.71	0.78	76	ATP, MG
2	91	0.44	0.79	17	empty

Compared structures

4QDI · Crystal structure II of MurF from Acinetobacter baumannii · the same entry in another collection · chain A against A, TM-score 1.00

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 B7GVN5
Elsewhere: RCSB PDB 4QDI · PDBe 4QDI · UniProt B7GVN5

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