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Crystal structure of human folate receptor alpha in complex with novel antifolate AGF183

Analyse Crystal structure of human folate receptor alpha in complex with novel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IZQ
Type: protein
Length: 1,649 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Folate receptor alpha
UniProt: P15328
Ligands: 83A
Pockets: 16 · best druggability 0.74

Structure

x-ray diffraction · 8 distinct chains · 33% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Folate receptor alpha	protein	207	32% helix, 9% strand	P15328
B	Folate receptor alpha	protein	203	33% helix, 8% strand	P15328
C	Folate receptor alpha	protein	208	34% helix, 11% strand	P15328
D	Folate receptor alpha	protein	209	32% helix, 11% strand	P15328
E	Folate receptor alpha	protein	206	33% helix, 11% strand	P15328
F	Folate receptor alpha	protein	208	32% helix, 11% strand	P15328
G	Folate receptor alpha	protein	205	33% helix, 12% strand	P15328
H	Folate receptor alpha	protein	203	33% helix, 9% strand	P15328

Ligands and binding sites

83A · N-(4-{[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]amino}benzene-1-carbonyl)-L-glutamic acid · ligand · 7 copies · chains A, B, C, D, E, F, G, H

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

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	201	0.74	0.89	29	empty
2	159	0.73	0.91	28	83A
3	194	0.73	0.89	28	83A
4	204	0.73	0.89	33	83A
5	195	0.73	0.89	29	83A

Interfaces

10 interfaces between chains.

C–F · 718 Å² buried · 14 hydrogen bonds · protein-protein
E–H · 680 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 680 Å² buried · 9 hydrogen bonds · protein-protein
D–G · 660 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 235 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 64 disulfide (disulfide).

Compared structures

5IZQ · Crystal structure of human folate receptor alpha in complex with novel antifolate AGF183 · the same entry in another collection · chain H against H, TM-score 1.00
P15328 · AlphaFold monomer V2.0 prediction for folate receptor alpha (P15328) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 5IZQ · PDBe 5IZQ · UniProt P15328

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