MolNFT v1 · #83577 · protein

Gale-like L-threonine dehydrogenase from cupriavidus necator (apo form)

3WMW · NAD dependent EPIMERASE/DEHYDRATASE: “Gale-like L-threonine dehydrogenase from cupriavidus necator (apo form)”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.65). MolNFT v1 #83577 on GenesisL1: 3D structure…

PDB: 3WMW
Type: protein
Length: 555 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NAD dependent EPIMERASE/DEHYDRATASE
EC: 1.-.-.-
UniProt: Q0K312
Ligands: CA
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD dependent EPIMERASE/DEHYDRATASE (EC 1.-.-.-)	protein	277	48% helix, 16% strand	Q0K312
B	NAD dependent EPIMERASE/DEHYDRATASE (EC 1.-.-.-)	protein	278	47% helix, 16% strand	Q0K312

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B

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

Pockets

3 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	384	0.65	0.79	41	empty
2	285	0.60	0.78	39	empty
3	52	0.27	0.74	16	CA

Interfaces

1 interface between chains.

A–B · 1172 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3WMW · GalE-like L-Threonine dehydrogenase from Cupriavidus necator (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 Q0K312
Elsewhere: RCSB PDB 3WMW · PDBe 3WMW · UniProt Q0K312

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