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Crystal structure analysis of low molecular weight protein tyrosine phosphatase from T. tengcongensis

Analyse Crystal structure analysis of low molecular weight protein tyrosine phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EGS
Type: protein
Length: 294 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribose 5-phosphate isomerase rpib
UniProt: Q8RD95
Ligands: BCT, NA
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribose 5-phosphate isomerase rpib	protein	147	44% helix, 14% strand	Q8RD95

Ligands and binding sites

BCT · Bicarbonate ion · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · chains 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	57	0.36	0.78	13	empty
2	54	0.29	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 457 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

4EGS · Crystal Structure Analysis of Low Molecular Weight Protein Tyrosine Phosphatase from T.… · 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 Q8RD95
Elsewhere: RCSB PDB 4EGS · PDBe 4EGS · UniProt Q8RD95

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