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Phloroglucinol reductase from clostridium sp. apo-form

Analyse Phloroglucinol reductase from clostridium sp. apo-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5G4K
Type: protein
Length: 528 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxidoreductase, short chain DEHYDROGENASE/REDUCTASE family protein
UniProt: U2C7W9
Pockets: 7 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxidoreductase, short chain DEHYDROGENASE/REDUCTASE family protein	protein	264	47% helix, 15% strand	U2C7W9
B	Oxidoreductase, short chain DEHYDROGENASE/REDUCTASE family protein	protein	264	48% helix, 15% strand	U2C7W9

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.64	0.79	46	empty
2	349	0.63	0.79	43	empty
3	164	0.54	0.80	22	empty
4	132	0.45	0.77	22	empty
5	90	0.36	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 2293 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5G4K · Phloroglucinol reductase from Clostridium sp. apo-form · 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 U2C7W9
Elsewhere: RCSB PDB 5G4K · PDBe 5G4K · UniProt U2C7W9

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