MolNFT v1 · #25526 · protein

Streptavidin complexed with cyclo-ac-[chpqgppc]-NH2 monomer, pH 2.85

1VWO: “Streptavidin complexed with cyclo-ac-[chpqgppc]-NH2 monomer, pH 2.85”. X-ray diffraction, 2 ligands (ACE, NH2). MolNFT v1 #25526 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1VWO
Type: protein
Length: 129 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Streptavidin; Peptide ligand containing hpq
UniProt: P22629
Ligands: ACE, NH2

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Streptavidin	protein	121	5% helix, 56% strand	P22629
P	Peptide ligand containing hpq	protein	8	0% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains B, P
NH2 · Amino group · ion · chains B, P

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

Interfaces

1 interface between chains.

B–P · 422 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

1VWO · Streptavidin complexed with cyclo-ac-[chpqgppc]-NH2 monomer, pH 2.85 · the same entry in another collection · chain P against P, 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 1VWO · PDBe 1VWO · UniProt P22629

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