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Crystal structure of DCOH2, a paralog of dcoh, the dimerization cofactor of hnf-1

Analyse Crystal structure of DCOH2, a paralog of dcoh, the dimerization cofactor of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RU0
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dcoh-like protein dcohm
EC: 4.2.1.96
UniProt: Q9CZL5
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dcoh-like protein dcohm (EC 4.2.1.96)	protein	100	45% helix, 23% strand	Q9CZL5
B	Dcoh-like protein dcohm (EC 4.2.1.96)	protein	98	46% helix, 21% strand	Q9CZL5

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.28	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 726 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1RU0 · Crystal structure of DCoH2, a paralog of DCoH, the Dimerization Cofactor of HNF-1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9CZL5 · AlphaFold monomer V2.0 prediction for pterin-4-alpha-carbinolamine dehydratase 2 (Q9CZL5) · a predicted model of the same protein · chain B 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 Q9CZL5
Elsewhere: RCSB PDB 1RU0 · PDBe 1RU0 · UniProt Q9CZL5

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