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Bacillus amyloliquefaciens CBM33 in complex with CU(I) reduced using ascorbate

Analyse Bacillus amyloliquefaciens CBM33 in complex with CU(I) reduced using ascorbate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YOY
Type: protein
Length: 356 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RBAM17540
EC: 1.-.-.-
UniProt: E1UUV3
Ligands: CU1
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	RBAM17540 (EC 1.-.-.-)	protein	178	22% helix, 38% strand	E1UUV3

Ligands and binding sites

CU1 · Copper (I) ion · metal · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 4 copies · chains A, B

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

Pockets

2 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	241	0.54	0.77	31	empty
2	78	0.35	0.76	20	empty

Interfaces

1 interface between chains.

A–B · 251 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2YOY · Bacillus amyloliquefaciens CBM33 in complex with Cu(I) reduced using ascorbate · 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 E1UUV3
Elsewhere: RCSB PDB 2YOY · PDBe 2YOY · UniProt E1UUV3

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