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Putative NAD-dependent EPIMERASE/DEHYDRATASE from bacillus halodurans.

Analyse Putative NAD-dependent EPIMERASE/DEHYDRATASE from bacillus halodurans. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3E8X
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative NAD-dependent EPIMERASE/DEHYDRATASE
UniProt: Q9KCP9
Ligands: NAP, CL
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative NAD-dependent EPIMERASE/DEHYDRATASE	protein	214	42% helix, 23% strand	Q9KCP9

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	429	0.68	0.80	47	NAP
2	54	0.26	0.73	16	CL

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

3E8X · Putative NAD-dependent epimerase/dehydratase from Bacillus halodurans. · 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 Q9KCP9
Elsewhere: RCSB PDB 3E8X · PDBe 3E8X · UniProt Q9KCP9

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