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Hit family hydrolase from clostridium thermocellum cth-393

Analyse Hit family hydrolase from clostridium thermocellum cth-393 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UVM
Type: protein
Length: 230 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histidine triad (hit) protein
UniProt: A3DF72
Ligands: ADN, ZN, UNX
Pockets: 2 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Histidine triad (hit) protein	protein	115	21% helix, 23% strand	A3DF72

Ligands and binding sites

ADN · Adenosine · ligand · chains B
ZN · Zinc ion · metal · 2 copies · chains A, B
UNX · Unknown atom or ion · ion · 31 copies · chains A, B

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	106	0.39	0.75	22	UNX, ADN
2	73	0.36	0.77	20	UNX

Interfaces

1 interface between chains.

A–B · 320 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

5UVM · HIT family hydrolase from Clostridium thermocellum Cth-393 · 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 A3DF72
Elsewhere: RCSB PDB 5UVM · PDBe 5UVM · UniProt A3DF72

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