MolNFT v1 · #39725 · protein

The crystal structure of class C acid phosphatase from bacillus anthracis with tungstate bound

2I34: “The crystal structure of class C acid phosphatase from bacillus anthracis with tungstate bound”. X-ray diffraction, 2 ligands (MG, WO4), 4 pockets (best druggability 0.69). MolNFT v1 #39725 on GenesisL1: 3D structure, binding sites…

PDB: 2I34
Type: protein
Length: 474 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acid phosphatase
EC: 3.1.3.2
UniProt: Q81L82
Ligands: MG, WO4
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acid phosphatase (EC 3.1.3.2)	protein	237	51% helix, 15% strand	Q81L82

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
WO4 · Tungstate(vi)ion · ion · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	453	0.69	0.80	45	MG, WO4
2	502	0.69	0.79	43	WO4
3	71	0.33	0.75	19	empty
4	75	0.31	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 2925 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

2I34 · The crystal structure of Class C acid phosphatase from Bacillus anthracis with tungstate… · 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 Q81L82
Elsewhere: RCSB PDB 2I34 · PDBe 2I34 · UniProt Q81L82

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