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Highly hydrated human vcam-1 fragment

Analyse Highly hydrated human vcam-1 fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IJ9
Type: protein
Length: 196 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vascular cell adhesion protein 1
UniProt: P19320
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vascular cell adhesion protein 1	protein	196	5% helix, 56% strand	P19320

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	72	0.32	0.75	19	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1IJ9 · Highly Hydrated Human VCAM-1 Fragment · the same entry in another collection · chain A against A, TM-score 1.00
P19320 · AlphaFold monomer V2.0 prediction for vascular cell adhesion protein 1 (P19320) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P19320
Elsewhere: RCSB PDB 1IJ9 · PDBe 1IJ9 · UniProt P19320

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