MolNFT v1 · #54381 · protein

Structure of menh from S. aureus

2XMZ · Hydrolase, ALPHA/BETA hydrolase fold family: “Structure of menh from S. aureus”. X-ray diffraction, 1 pocket (best druggability 0.71). MolNFT v1 #54381 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2XMZ
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrolase, ALPHA/BETA hydrolase fold family
EC: 4.2.99.20
UniProt: Q5HH39
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrolase, ALPHA/BETA hydrolase fold family (EC 4.2.99.20)	protein	266	50% helix, 15% strand	Q5HH39

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	304	0.71	0.84	52	empty

Compared structures

2XMZ · Structure of MenH from S. aureus · 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 Q5HH39
Elsewhere: RCSB PDB 2XMZ · PDBe 2XMZ · UniProt Q5HH39

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