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The 1.7 ångström crystal structure of bpi

Analyse The 1.7 ångström crystal structure of bpi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EWF
Type: protein
Length: 456 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BACTERICIDAL/PERMEABILITY-increasing protein
UniProt: P17213
Ligands: PC1
Pockets: 2 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BACTERICIDAL/PERMEABILITY-increasing protein	protein	456	25% helix, 45% strand	P17213

Ligands and binding sites

PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	557	0.85	0.90	59	PC1
2	461	0.83	0.89	45	PC1

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1EWF · The 1.7 ångström crystal structure of bpi · the same entry in another collection · chain A against A, TM-score 1.00
P17213 · AlphaFold monomer V2.0 prediction for bactericidal permeability- increasing protein… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P17213
Elsewhere: RCSB PDB 1EWF · PDBe 1EWF · UniProt P17213

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