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Crystal structure of a mammalian reductase

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

PDB: 2ZAT
Type: protein
Length: 1,004 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.5
Source: Sus scrofa
Molecule: Dehydrogenase/reductase SDR family member 4
EC: 1.1.1.184
UniProt: Q8WNV7
Ligands: NAP
Pockets: 12 · best druggability 0.79

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 51% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184)	protein	251	51% helix, 16% strand	Q8WNV7

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D

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

Pockets

12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	615	0.79	0.84	89	empty
2	494	0.76	0.84	73	empty
3	424	0.75	0.85	50	NAP
4	400	0.75	0.85	42	NAP
5	407	0.74	0.84	42	NAP

Interfaces

6 interfaces between chains.

A–D · 1604 Å² buried · 32 hydrogen bonds · protein-protein
B–C · 1579 Å² buried · 30 hydrogen bonds · protein-protein
C–D · 1543 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 1540 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 376 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2ZAT · Crystal structure of a mammalian reductase · the same entry in another collection · chain D against D, TM-score 1.00
Q8WNV7 · AlphaFold monomer V2.0 prediction for DEHYDROGENASE/REDUCTASE sdr family member 4 (Q8WNV7) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q8WNV7
Elsewhere: RCSB PDB 2ZAT · PDBe 2ZAT · UniProt Q8WNV7

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