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Unusual structural features in the parallel beta-helix in pectate lyases

Analyse Unusual structural features in the parallel beta-helix in pectate lyases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PCL
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pectate lyase E
EC: 4.2.2.2
UniProt: P04960
Pockets: 2 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Pectate lyase E (EC 4.2.2.2)	protein	355	0% helix, 0% strand	P04960

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	79	0.33	0.72	22	empty
2	60	0.30	0.73	20	empty

Compared structures

1PCL · Unusual structural features in the parallel beta-helix in pectate lyases · the same entry in another collection · chain A against A, TM-score 1.00
P04960 · AlphaFold monomer V2.0 prediction for pectate lyase E (P04960) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P04960
Elsewhere: RCSB PDB 1PCL · PDBe 1PCL · UniProt P04960

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