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Crystal structure of the zea mays laccase 3

Analyse Crystal structure of the zea mays laccase 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KLG
Type: protein
Length: 547 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Laccase
EC: 1.10.3.2
UniProt: Q2PAJ1
Ligands: NAG, CU, OXY
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Laccase (EC 1.10.3.2)	protein	547	11% helix, 40% strand	Q2PAJ1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
CU · Copper (II) ion · metal · 4 copies · chains A
OXY · Oxygen molecule · ion · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	151	0.68	0.88	37	empty
2	218	0.61	0.82	34	empty
3	217	0.53	0.77	36	empty
4	53	0.46	0.84	17	NAG
5	68	0.37	0.78	16	empty

Modifications

Observed in the structure: 7 glycan, 3 disulfide (N-glycosylation, disulfide).

Compared structures

6KLG · Crystal Structure of the Zea Mays laccase 3 · 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 Q2PAJ1
Elsewhere: RCSB PDB 6KLG · PDBe 6KLG · UniProt Q2PAJ1

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