MolNFT v1 · #102389 · protein

Structural-, kinetic- and docking studies of artificial imine reductases based on the biotin-streptavidin technology: an induced lock-and-key hypothesis

4OKA: “Structural-, kinetic- and docking studies of artificial imine reductases based on the biotin-streptavidin…”. X-ray diffraction, 2 ligands (5IR, IR), 1 pocket (best druggability 0.49). MolNFT v1 #102389 on GenesisL1: 3D structure…

PDB: 4OKA
Type: protein
Length: 122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: 5IR, IR
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	122	8% helix, 55% strand	P22629

Ligands and binding sites

5IR · [N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamidato]iridium(III) · ligand · chains A
IR · Iridium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	91	0.49	0.82	17	5IR

Compared structures

4OKA · Structural-, Kinetic- and Docking Studies of Artificial Imine Reductases Based on the… · 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 P22629
Elsewhere: RCSB PDB 4OKA · PDBe 4OKA · UniProt P22629

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