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The structure of ribose 5-phosphate isomerase B from anaplasma phagocytophilum

Analyse The structure of ribose 5-phosphate isomerase B from anaplasma phagocytophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EM8
Type: protein
Length: 291 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribose 5-phosphate isomerase B
EC: 5.3.1.6
UniProt: Q2GK74
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribose 5-phosphate isomerase B (EC 5.3.1.6)	protein	146	44% helix, 18% strand	Q2GK74
B	Ribose 5-phosphate isomerase B (EC 5.3.1.6)	protein	145	43% helix, 18% strand	Q2GK74

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.57	0.82	34	empty
2	63	0.47	0.84	15	empty
3	57	0.44	0.83	14	empty
4	55	0.32	0.76	12	empty

Interfaces

1 interface between chains.

A–B · 1429 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

4EM8 · The Structure of Ribose 5-phosphate Isomerase B from Anaplasma phagocytophilum · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q2GK74
Elsewhere: RCSB PDB 4EM8 · PDBe 4EM8 · UniProt Q2GK74

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