Research workbench

Structure of dimeric human glycodelin

Analyse Structure of dimeric human glycodelin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4R0B
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycodelin
UniProt: P09466
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycodelin	protein	153	12% helix, 45% strand	P09466

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	148	0.50	0.78	23	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4R0B · Structure of dimeric human glycodelin · the same entry in another collection · chain A against A, TM-score 1.00
P09466 · AlphaFold monomer V2.0 prediction for glycodelin (P09466) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P09466
Elsewhere: RCSB PDB 4R0B · PDBe 4R0B · UniProt P09466

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.