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Zn-alpha-2-glycoprotein; baculo-zag peg 200

Analyse Zn-alpha-2-glycoprotein; baculo-zag peg 200 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T7V
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Zinc-alpha-2-glycoprotein
UniProt: P25311
Ligands: NAG
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zinc-alpha-2-glycoprotein	protein	273	25% helix, 43% strand	P25311

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
P6G · Hexaethylene glycol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	238	0.59	0.79	19	P6G
2	62	0.37	0.78	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1T7V · Zn-alpha-2-glycoprotein; baculo-ZAG PEG 200 · the same entry in another collection · chain A against A, TM-score 1.00
P25311 · AlphaFold monomer V2.0 prediction for zinc-alpha-2-glycoprotein (P25311) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P25311
Elsewhere: RCSB PDB 1T7V · PDBe 1T7V · UniProt P25311

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