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The refined three-dimensional structure of pectate lyase C from erwinia chrysanthemi at 2.2 ångströms resolution: implications for an enzymatic mechanism

Analyse The refined three-dimensional structure of pectate lyase C from erwinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2PEC
Type
protein
Length
352 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pectate lyase C
EC
4.2.2.2
UniProt
P11073
Pockets
1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APectate lyase C (EC 4.2.2.2)protein35213% helix, 34% strandP11073

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1810.320.7419empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2PEC · The refined three-dimensional structure of pectate lyase C from erwinia chrysanthemi at… · the same entry in another collection · chain A against A, TM-score 1.00
  • P11073 · AlphaFold monomer V2.0 prediction for pectate lyase C (P11073) · a predicted model of the same protein · chain A against A, TM-score 1.00

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