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Crystal structure of glucuronic acid dehydrogeanse from chromohalobacter salexigens

Analyse Crystal structure of glucuronic acid dehydrogeanse from chromohalobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AY3
Type: protein
Length: 1,064 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD-dependent EPIMERASE/DEHYDRATASE
UniProt: Q1QUN7
Pockets: 10 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	NAD-dependent EPIMERASE/DEHYDRATASE	protein	266	41% helix, 17% strand	Q1QUN7

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	889	0.83	0.85	117	empty
2	419	0.71	0.82	45	empty
3	426	0.70	0.82	44	empty
4	384	0.62	0.78	57	empty
5	292	0.59	0.78	40	empty

Interfaces

3 interfaces between chains.

C–D · 1484 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1480 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 337 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3AY3 · Crystal structure of glucuronic acid dehydrogeanse from Chromohalobacter salexigens · 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 Q1QUN7
Elsewhere: RCSB PDB 3AY3 · PDBe 3AY3 · UniProt Q1QUN7

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