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Cellobiose phosphorylase from cellulomonas uda in complex with glucose

Analyse Cellobiose phosphorylase from cellulomonas uda in complex with glucose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S4B
Type: protein
Length: 1,644 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellobiose phosphorylase
EC: 2.4.1.20
UniProt: Q7WTR6
Ligands: GLC
Pockets: 15 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cellobiose phosphorylase (EC 2.4.1.20)	protein	822	30% helix, 27% strand	Q7WTR6

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B

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

Pockets

15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	161	0.80	0.96	33	empty
2	595	0.78	0.84	52	GLC
3	576	0.77	0.84	57	GLC
4	159	0.68	0.88	32	empty
5	151	0.67	0.88	32	empty

Interfaces

1 interface between chains.

A–B · 3343 Å² buried · 56 hydrogen bonds · protein-protein

Compared structures

3S4B · Cellobiose phosphorylase from Cellulomonas uda in complex with glucose · 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 Q7WTR6
Elsewhere: RCSB PDB 3S4B · PDBe 3S4B · UniProt Q7WTR6

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