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Crystal structure of vanadium-dependent haloperoxidase from a. marina

Analyse Crystal structure of vanadium-dependent haloperoxidase from a. marina in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LPC
Type: protein
Length: 624 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vanadium-dependent bromoperoxidase
UniProt: B0C4R0
Ligands: PO4
Pockets: 7 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vanadium-dependent bromoperoxidase	protein	624	40% helix, 10% strand	B0C4R0

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	204	0.52	0.77	27	PO4
2	136	0.50	0.80	32	empty
3	79	0.36	0.76	15	empty
4	75	0.34	0.75	17	empty
5	75	0.33	0.75	22	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5LPC · Crystal structure of Vanadium-dependent Haloperoxidase from A. marina · 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 B0C4R0
Elsewhere: RCSB PDB 5LPC · PDBe 5LPC · UniProt B0C4R0

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