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Crystal structure of putative metal-dependent hydrolase (YP_805737.1) from lactobacillus casei atcc 334 at 1.40 a resolution

Analyse Crystal structure of putative metal-dependent hydrolase (YP_805737.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QPX
Type: protein
Length: 376 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Predicted metal-dependent hydrolase of the tim-barrel fold
UniProt: Q03BX7
Ligands: ZN
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Predicted metal-dependent hydrolase of the tim-barrel fold	protein	376	53% helix, 11% strand	Q03BX7

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 11 copies · chains A

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

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	350	0.61	0.78	33	empty

Modifications

Observed in the structure: 9 modified (engineered, carboxylation).

Compared structures

2QPX · Crystal structure of putative metal-dependent hydrolase (YP_805737.1) from Lactobacillus… · 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 Q03BX7
Elsewhere: RCSB PDB 2QPX · PDBe 2QPX · UniProt Q03BX7

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