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Crystal structure of TM1679, a metal-dependent hydrolase of the beta- lactamase superfamily

Analyse Crystal structure of TM1679, a metal-dependent hydrolase of the beta- lactamase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3H3E
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein TM1679
UniProt: Q9X207
Ligands: ZN
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein TM1679	protein	256	23% helix, 31% strand	Q9X207

Ligands and binding sites

ZN · Zinc ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.50	0.87	18	empty
2	89	0.40	0.78	20	empty

Modifications

Observed in the structure: 4 modified, 2 disulfide (engineered, disulfide).

Compared structures

3H3E · Crystal structure of Tm1679, A METAL-DEPENDENT HYDROLASE OF THE BETA-LACTAMASE SUPERFAMILY · 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 Q9X207
Elsewhere: RCSB PDB 3H3E · PDBe 3H3E · UniProt Q9X207

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