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Crystal structure of LAC15 from a marine microbial metagenome

Analyse Crystal structure of LAC15 from a marine microbial metagenome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F7K
Type: protein
Length: 750 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Laccase
EC: 1.10.3.2
UniProt: E1ACR6
Pockets: 9 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Laccase (EC 1.10.3.2)	protein	377	2% helix, 50% strand	E1ACR6
B	Laccase (EC 1.10.3.2)	protein	373	2% helix, 50% strand	E1ACR6

Ligands and binding sites

GOL · Glycerol · additive · 5 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	996	0.80	0.82	87	empty
2	202	0.72	0.88	35	empty
3	157	0.71	0.90	32	empty
4	117	0.41	0.75	32	GOL
5	104	0.37	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 1195 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4F7K · Crystal structure of Lac15 from a marine microbial metagenome · 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 E1ACR6
Elsewhere: RCSB PDB 4F7K · PDBe 4F7K · UniProt E1ACR6

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