MolNFT v1 · #77091 · protein

Divergence of structure and function among phosphatases of the haloalkanoate (had) enzyme superfamily: analysis of BT1666 from bacteroides thetaiotaomicron

3R4C · Hydrolase, haloacid dehalogenase-like hydrolase: “Divergence of structure and function among phosphatases of the haloalkanoate (had) enzyme superfamily…”. X-ray diffraction, 2 ligands (MG, SO4), 1 pocket (best druggability 0.66).…

PDB: 3R4C
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hydrolase, haloacid dehalogenase-like hydrolase
UniProt: Q8A759
Ligands: MG, SO4
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hydrolase, haloacid dehalogenase-like hydrolase	protein	268	35% helix, 23% strand	Q8A759

Ligands and binding sites

MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · 3 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	552	0.66	0.77	44	MG, SO4

Compared structures

3R4C · Divergence of Structure and Function Among Phosphatases of the Haloalkanoate (HAD) Enzyme… · 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 Q8A759
Elsewhere: RCSB PDB 3R4C · PDBe 3R4C · UniProt Q8A759

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