Research workbench

Human zinc-alpha-2-glycoprotein

Analyse Human zinc-alpha-2-glycoprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZAG
Type: protein
Length: 1,083 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P25311

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	273	—	P25311
B	—	protein	274	—	P25311
C	—	protein	273	—	P25311
D	—	protein	263	—	P25311

Compared structures

1ZAG · Human zinc-alpha-2-glycoprotein · the same entry in another collection · chain D against D, TM-score 1.00
P25311 · AlphaFold monomer V2.0 prediction for zinc-alpha-2-glycoprotein (P25311) · a predicted model of the same protein · chain B 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 P25311
Elsewhere: RCSB PDB 1ZAG · PDBe 1ZAG · UniProt P25311

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