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Atomic resolution structure of hbp

Analyse Atomic resolution structure of hbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1A7S
Type: protein
Length: 221 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heparin binding protein
UniProt: P20160
Ligands: NAG, CL
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heparin binding protein	protein	221	9% helix, 38% strand	P20160

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
CL · Chloride ion · ion · chains A
EOH · Ethanol · additive · 15 copies · 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	75	0.32	0.74	16	EOH

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

1A7S · Atomic resolution structure of hbp · the same entry in another collection · chain A against A, TM-score 1.00
P20160 · AlphaFold monomer V2.0 prediction for azurocidin (P20160) · a predicted model of the same protein · 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 P20160
Elsewhere: RCSB PDB 1A7S · PDBe 1A7S · UniProt P20160

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