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Substituting the prolines of 4-oxalocrotonate tautomerase with non- canonical analogue (2S)-3,4-dehydroproline

Analyse Substituting the prolines of 4-oxalocrotonate tautomerase with non- canonical… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GHW
Type: protein
Length: 171 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-hydroxymuconate tautomerase
EC: 5.3.2.6
UniProt: Q01468
Ligands: CA

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	2-hydroxymuconate tautomerase (EC 5.3.2.6)	protein	57	39% helix, 32% strand	Q01468

Ligands and binding sites

CA · Calcium ion · metal · chains C

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

Interfaces

2 interfaces between chains.

A–B · 922 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 195 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (nonstandard).

Compared structures

6GHW · Substituting the prolines of 4-oxalocrotonate tautomerase with non-canonical analogue… · the same entry in another collection · chain A against A, TM-score 1.00
Q01468 · AlphaFold monomer V2.0 prediction for 2-hydroxymuconate tautomerase (Q01468) · a predicted model of the same protein · chain B against A, TM-score 0.93

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 Q01468
Elsewhere: RCSB PDB 6GHW · PDBe 6GHW · UniProt Q01468

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