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Crystal structure of L-threonine dehydrogenase from hyperthermophilic archaeon thermoplasma volcanium

Analyse Crystal structure of L-threonine dehydrogenase from hyperthermophilic archaeon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3A1N
Type: protein
Length: 624 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ndp-sugar epimerase
EC: 1.1.1.103
UniProt: Q97BK3
Ligands: NAD
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ndp-sugar epimerase (EC 1.1.1.103)	protein	315	44% helix, 17% strand	Q97BK3
B	Ndp-sugar epimerase (EC 1.1.1.103)	protein	309	44% helix, 18% strand	Q97BK3

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

2 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	417	0.76	0.85	50	NAD
2	437	0.76	0.85	51	NAD

Interfaces

1 interface between chains.

A–B · 1387 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3A1N · Crystal structure of L-Threonine dehydrogenase from Hyperthermophilic Archaeon… · 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 Q97BK3
Elsewhere: RCSB PDB 3A1N · PDBe 3A1N · UniProt Q97BK3

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