Research workbench

Pectate lyase C from erwinia chrysanthemi with 1 LU+3 ion in the putative calcium binding site

Analyse Pectate lyase C from erwinia chrysanthemi with 1 LU+3 ion in the putative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PLU
Type: protein
Length: 352 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (pectate lyase C)
EC: 4.2.2.2
UniProt: P11073
Ligands: LU
Pockets: 1 · best druggability 0.31

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (pectate lyase C) (EC 4.2.2.2)	protein	352	13% helix, 34% strand	P11073

Ligands and binding sites

LU · Lutetium (III) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.31	0.74	20	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1PLU · Pectate lyase C from erwinia chrysanthemi with 1 LU+3 ion in the putative calcium binding… · 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

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 P11073
Elsewhere: RCSB PDB 1PLU · PDBe 1PLU · UniProt P11073

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