MolNFT v1 · #147877 · protein

Crystal structure of a polyethylene terephthalate degrading hydrolase from ideonella sakaiensis collected at long wavelength

6EQD · POLY(ETHYLENE terephthalate) hydrolase: “Crystal structure of a polyethylene terephthalate degrading hydrolase from ideonella sakaiensis collected at…”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #147877 on GenesisL1: 3D structure…

PDB: 6EQD
Type: protein
Length: 790 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLY(ETHYLENE terephthalate) hydrolase
EC: 3.1.1.101
UniProt: A0A0K8P6T7
Ligands: CL

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 23% strand (DSSP).

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

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains B, C

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

Interfaces

2 interfaces between chains.

A–B · 630 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 600 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

6EQD · 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 6EQD · PDBe 6EQD · UniProt A0A0K8P6T7

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