Research workbench

Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis in spacegroup C2221

Analyse Crystal structure of a polyethylene terephthalate degrading hydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EQH
Type: protein
Length: 789 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.58
Source: Ideonella sakaiensis (strain 201-F6)
Molecule: Poly(ethylene terephthalate) hydrolase
EC: 3.1.1.101
UniProt: A0A0K8P6T7

Structure

x-ray diffraction · resolution 1.58 · 3 distinct chains · 29% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Poly(ethylene terephthalate) hydrolase (EC 3.1.1.101)	protein	263	29% helix, 23% strand	A0A0K8P6T7
B	Poly(ethylene terephthalate) hydrolase (EC 3.1.1.101)	protein	264	29% helix, 22% strand	A0A0K8P6T7
C	Poly(ethylene terephthalate) hydrolase (EC 3.1.1.101)	protein	262	30% helix, 23% strand	A0A0K8P6T7

Interfaces

1 interface between chains.

A–B · 615 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

6EQH · Crystal structure of a polyethylene terephthalate degrading hydrolase from ideonella… · the same entry in another collection · chain A 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 A0A0K8P6T7
Elsewhere: RCSB PDB 6EQH · PDBe 6EQH · UniProt A0A0K8P6T7

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