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Structure of the M298F mutant of the streptomyces coelicolor small laccase T1 copper axial ligand.

Analyse Structure of the M298F mutant of the streptomyces coelicolor small laccase T1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7B2K
Type: protein
Length: 562 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative copper oxidase
UniProt: Q9XAL8
Ligands: CU
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative copper oxidase	protein	282	5% helix, 41% strand	Q9XAL8
B	Putative copper oxidase	protein	280	5% helix, 41% strand	Q9XAL8

Ligands and binding sites

CU · Copper (II) ion · metal · 8 copies · chains A, B

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

Pockets

3 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	684	0.62	0.73	79	empty
2	70	0.34	0.76	14	empty
3	67	0.34	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 1145 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

7B2K · Structure of the M298F mutant of the Streptomyces coelicolor small laccase T1 copper… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9XAL8
Elsewhere: RCSB PDB 7B2K · PDBe 7B2K · UniProt Q9XAL8

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