Research workbench

Crystal structure of human DHRS6

Analyse Crystal structure of human DHRS6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AG5
Type: protein
Length: 979 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DEHYDROGENASE/REDUCTASE (sdr family) member 6
UniProt: Q9BUT1
Ligands: NAD, SO4
Pockets: 11 · best druggability 0.87

Structure

x-ray diffraction · 3 distinct chains · 50% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DEHYDROGENASE/REDUCTASE (sdr family) member 6	protein	246	50% helix, 18% strand	Q9BUT1
B	DEHYDROGENASE/REDUCTASE (sdr family) member 6	protein	245	50% helix, 18% strand	Q9BUT1
C, D	DEHYDROGENASE/REDUCTASE (sdr family) member 6	protein	244	49% helix, 18% strand	Q9BUT1

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	974	0.87	0.87	71	empty
2	450	0.77	0.86	59	SO4, NAD
3	374	0.76	0.86	43	SO4, NAD
4	364	0.75	0.86	44	SO4, NAD
5	373	0.74	0.85	44	SO4, NAD

Interfaces

6 interfaces between chains.

B–C · 1698 Å² buried · 26 hydrogen bonds · protein-protein
A–D · 1693 Å² buried · 26 hydrogen bonds · protein-protein
A–B · 1348 Å² buried · 12 hydrogen bonds · protein-protein
C–D · 1333 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 190 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2AG5 · Crystal Structure of Human DHRS6 · the same entry in another collection · chain D against D, TM-score 1.00
Q9BUT1 · AlphaFold monomer V2.0 prediction for 3-hydroxybutyrate dehydrogenase type 2 (Q9BUT1) · a predicted model of the same protein · chain D 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 Q9BUT1
Elsewhere: RCSB PDB 2AG5 · PDBe 2AG5 · UniProt Q9BUT1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.