Research workbench

D67R mutant of D-ribose-binding protein from escherichia COLI

Analyse D67R mutant of D-ribose-binding protein from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BA2
Type: protein
Length: 542 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-ribose-binding protein
UniProt: P02925
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	D-ribose-binding protein	protein	271	46% helix, 21% strand	P02925

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	420	0.60	0.76	41	empty
2	178	0.53	0.79	30	empty
3	243	0.49	0.74	26	empty
4	57	0.26	0.73	12	empty

Interfaces

1 interface between chains.

A–B · 297 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1BA2 · D67R mutant of D-ribose-binding protein from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
P02925 · AlphaFold monomer V2.0 prediction for ribose import binding protein rbsb (P02925) · a predicted model of the same protein · chain A against A, TM-score 0.65

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 P02925
Elsewhere: RCSB PDB 1BA2 · PDBe 1BA2 · UniProt P02925

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