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Crystal structure of laccasse from thermus thermophilus HB27 (ascorbic acid 10 min)

Analyse Crystal structure of laccasse from thermus thermophilus HB27 (ascorbic acid 10… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5K5K
Type: protein
Length: 439 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Laccase
EC: 1.10.3.2
UniProt: Q72HW2
Ligands: CU
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Laccase (EC 1.10.3.2)	protein	439	6% helix, 48% strand	Q72HW2

Ligands and binding sites

CU · Copper (II) ion · metal · 3 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 12 copies · chains A

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

Pockets

5 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	270	0.62	0.80	30	MPD
2	139	0.46	0.77	24	MPD
3	100	0.41	0.77	21	empty
4	94	0.38	0.76	21	empty
5	56	0.27	0.73	16	empty

Compared structures

5K5K · Crystal structure of laccasse from Thermus thermophilus HB27 (ascorbic acid 10 min) · 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 Q72HW2
Elsewhere: RCSB PDB 5K5K · PDBe 5K5K · UniProt Q72HW2

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