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Human transferrin N-lobe mutant H249Q

Analyse Human transferrin N-lobe mutant H249Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JQF
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transferrin
UniProt: P02787
Ligands: FE, K, CO3
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transferrin	protein	329	36% helix, 20% strand	P02787

Ligands and binding sites

FE · Fe (III) ion · metal · chains A
K · Potassium ion · metal · chains A
CO3 · Carbonate ion · ion · chains A

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

Pockets

3 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	211	0.73	0.89	41	empty
2	56	0.37	0.80	13	empty
3	80	0.34	0.75	13	empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1JQF · Human Transferrin N-Lobe Mutant H249Q · the same entry in another collection · chain A against A, TM-score 1.00
P02787 · AlphaFold monomer V2.0 prediction for serotransferrin (P02787) · a predicted model of the same protein · chain A 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 P02787
Elsewhere: RCSB PDB 1JQF · PDBe 1JQF · UniProt P02787

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