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Crystal structure of pseudomonas aeruginosa lytic polysaccharide monooxygenase cbpd

Analyse Crystal structure of pseudomonas aeruginosa lytic polysaccharide monooxygenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7SQX
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitin-binding protein cbpd
UniProt: Q9I589
Ligands: NH4
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitin-binding protein cbpd	protein	296	16% helix, 33% strand	Q9I589

Ligands and binding sites

NH4 · Ammonium ion · ion · 3 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	397	0.62	0.77	54	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

7SQX · Crystal Structure of Pseudomonas aeruginosa lytic polysaccharide monooxygenase CbpD · the same entry in another collection · chain A against A, TM-score 1.00
Q9I589 · AlphaFold monomer V2.0 prediction for chitin-binding protein cbpd (Q9I589) · a predicted model of the same protein · chain A against A, TM-score 0.64

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 Q9I589
Elsewhere: RCSB PDB 7SQX · PDBe 7SQX · UniProt Q9I589

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