MolNFT v1 · #85112 · protein

Coriolopsis gallica laccase T2 copper depleted at pH 4.5

4A2D: “Coriolopsis gallica laccase T2 copper depleted at pH 4.5”. X-ray diffraction, 3 ligands (NAG, BMA, CU), 4 pockets (best druggability 0.53). MolNFT v1 #85112 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4A2D
Type: protein
Length: 495 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Laccase
EC: 1.10.3.2
UniProt: Q1W6B1
Ligands: NAG, BMA, CU
Pockets: 4 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Laccase (EC 1.10.3.2)	protein	495	11% helix, 37% strand	Q1W6B1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
BMA · beta-D-mannopyranose · sugar · 3 copies · chains A
CU · Copper (II) ion · metal · 3 copies · chains A

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

Pockets

4 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	115	0.53	0.82	16	empty
2	167	0.48	0.76	28	empty
3	111	0.47	0.79	21	empty
4	62	0.42	0.82	17	empty

Modifications

Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

4A2D · Coriolopsis gallica Laccase T2 Copper Depleted at pH 4.5 · 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 Q1W6B1
Elsewhere: RCSB PDB 4A2D · PDBe 4A2D · UniProt Q1W6B1

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