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The crystal structure of ydce, a 4-oxalocrotonate tautomerase homologue from escherichia COLI, confirms the structural basis for oligomer diversity

Analyse The crystal structure of ydce, a 4-oxalocrotonate tautomerase homologue from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GYX
Type: protein
Length: 152 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein ydce
EC: 5.3.2.1
UniProt: P31992
Ligands: BEZ

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein ydce (EC 5.3.2.1)	protein	76	45% helix, 17% strand	P31992

Ligands and binding sites

BEZ · Benzoic acid · ligand · chains A, B
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A, B

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

Interfaces

1 interface between chains.

A–B · 1892 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

1GYX · The Crystal Structure of YdcE, a 4-Oxalocrotonate Tautomerase Homologue from Escherichia… · the same entry in another collection · chain A against A, TM-score 1.00
P31992 · AlphaFold monomer V2.0 prediction for tautomerase ppta (P31992) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P31992
Elsewhere: RCSB PDB 1GYX · PDBe 1GYX · UniProt P31992

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