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The structure of rice weevil pectin methyl esterase

Analyse The structure of rice weevil pectin methyl esterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PMH
Type: protein
Length: 366 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pectinesterase
EC: 3.1.1.11
UniProt: E7CIP7

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pectinesterase (EC 3.1.1.11)	protein	366	15% helix, 31% strand	E7CIP7

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4PMH · The structure of rice weevil pectin methyl esterase · the same entry in another collection · chain A against A, TM-score 1.00
E7CIP7 · AlphaFold monomer V2.0 prediction for pectinesterase (E7CIP7) · a predicted model of the same protein · 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 E7CIP7
Elsewhere: RCSB PDB 4PMH · PDBe 4PMH · UniProt E7CIP7

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