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Structural basis of the specific activity and thermostability of pectate lyase (peln) from paenibacillus sp. 0602

Analyse Structural basis of the specific activity and thermostability of pectate lyase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GT5
Type: protein
Length: 888 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pectate lyase
EC: 4.2.2.2
UniProt: W8CR80
Pockets: 5 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pectate lyase (EC 4.2.2.2)	protein	444	20% helix, 28% strand	W8CR80

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	240	0.66	0.84	42	empty
2	126	0.47	0.79	20	empty
3	162	0.45	0.75	29	empty
4	65	0.35	0.77	16	empty
5	51	0.30	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 612 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5GT5 · Structural basis of the specific activity and thermostability of pectate lyase (pelN)… · 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 W8CR80
Elsewhere: RCSB PDB 5GT5 · PDBe 5GT5 · UniProt W8CR80

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