MolNFT v1 · #97679 · protein

Human folate receptor alpha (FOLR1) at acidic pH, orthorhombic form

4KM6: “Human folate receptor alpha (FOLR1) at acidic pH, orthorhombic form”. X-ray diffraction, 2 ligands (NAG, CA), 1 pocket (best druggability 0.54). MolNFT v1 #97679 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4KM6
Type: protein
Length: 204 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Folate receptor alpha
UniProt: P15328
Ligands: NAG, CA
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Folate receptor alpha	protein	204	28% helix, 10% strand	P15328

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
CA · Calcium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	189	0.54	0.79	21	NAG

Modifications

Observed in the structure: 8 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

4KM6 · Human folate receptor alpha (FOLR1) at acidic pH, orthorhombic form · the same entry in another collection · chain A against A, TM-score 1.00
P15328 · AlphaFold monomer V2.0 prediction for folate receptor alpha (P15328) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 P15328
Elsewhere: RCSB PDB 4KM6 · PDBe 4KM6 · UniProt P15328

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