MolNFT v1 · #105299 · protein

Crystal structure of P. aeruginosa tpba (C132S) in complex with ptyr

4R0T · Protein tyrosine phosphatase tpba: “Crystal structure of P. aeruginosa tpba (C132S) in complex with ptyr”. X-ray diffraction, 2 ligands (TYR, PO4), 2 pockets (best druggability 0.47). MolNFT v1 #105299 on GenesisL1: 3D structure…

PDB: 4R0T
Type: protein
Length: 327 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein tyrosine phosphatase tpba
UniProt: Q9HXC7
Ligands: TYR, PO4
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Protein tyrosine phosphatase tpba	protein	162	46% helix, 15% strand	Q9HXC7
A	Protein tyrosine phosphatase tpba	protein	165	45% helix, 15% strand	Q9HXC7

Ligands and binding sites

TYR · Tyrosine · ligand · chains B
PO4 · Phosphate ion · ion · 2 copies · chains B, 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	90	0.47	0.81	13	empty
2	87	0.37	0.77	25	empty

Interfaces

1 interface between chains.

B–A · 431 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4R0T · Crystal structure of P. aeruginosa TpbA (C132S) in complex with pTyr · the same entry in another collection · chain B against B, 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 Q9HXC7
Elsewhere: RCSB PDB 4R0T · PDBe 4R0T · UniProt Q9HXC7

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