MolNFT v1 · #67728 · protein

Crystal structure of ligand-free francisella tularensis histidine acid phosphatase

3IT2: “Crystal structure of ligand-free francisella tularensis histidine acid phosphatase”. X-ray diffraction, 2 pockets (best druggability 0.67). MolNFT v1 #67728 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3IT2
Type: protein
Length: 656 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acid phosphatase
EC: 3.1.3.2
UniProt: Q2A612
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acid phosphatase (EC 3.1.3.2)	protein	329	46% helix, 15% strand	Q2A612
B	Acid phosphatase (EC 3.1.3.2)	protein	327	46% helix, 15% strand	Q2A612

Ligands and binding sites

ACT · Acetate ion · additive · 4 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	349	0.67	0.81	35	ACT
2	352	0.65	0.80	38	ACT

Interfaces

1 interface between chains.

A–B · 1770 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

3IT2 · Crystal structure of ligand-free Francisella tularensis histidine acid phosphatase · 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 Q2A612
Elsewhere: RCSB PDB 3IT2 · PDBe 3IT2 · UniProt Q2A612

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