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Crystal structure of okadaic acid binding protein 2.1

Analyse Crystal structure of okadaic acid binding protein 2.1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WRI
Type: protein
Length: 187 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Okadaic acid binding protein 2-alpha
UniProt: Q2MHR1
Ligands: OKA
Pockets: 1 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Okadaic acid binding protein 2-alpha	protein	187	63% helix, 5% strand	Q2MHR1

Ligands and binding sites

OKA · Okadaic acid · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	865	0.85	0.86	63	OKA

Modifications

Observed in the structure: 16 modified (methylation).

Compared structures

4WRI · Crystal structure of okadaic acid binding protein 2.1 · 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 Q2MHR1
Elsewhere: RCSB PDB 4WRI · PDBe 4WRI · UniProt Q2MHR1

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