MolNFT v1 · #137327 · protein

Coordination chemistry within a protein host: regulation of the secondary coordination sphere

5VL5 · Streptavidin: “Coordination chemistry within a protein host: regulation of the secondary coordination sphere”. X-ray diffraction, 2 ligands (S31, CU), 1 pocket (best druggability 0.48). MolNFT v1 #137327 on GenesisL1: 3D structure…

PDB: 5VL5
Type: protein
Length: 121 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin
UniProt: P22629
Ligands: S31, CU
Pockets: 1 · best druggability 0.48

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Streptavidin	protein	121	8% helix, 55% strand	P22629

Ligands and binding sites

S31 · [N-(3-{bis[2-(pyridin-2-yl-kappaN)ethyl]amino-kappaN}propyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide](azido)(hydroxy)copper · ligand · chains A
CU · Copper (II) 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	95	0.48	0.81	19	S31

Compared structures

5VL5 · Coordination Chemistry within a Protein Host: Regulation of the Secondary Coordination… · 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 5VL5 · PDBe 5VL5 · UniProt P22629

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