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Crystal structure of human serum transferrin, N-lobe L66W mutant

Analyse Crystal structure of human serum transferrin, N-lobe L66W mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1N7W
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serotransferrin
UniProt: P02787
Ligands: FE, CO3
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serotransferrin	protein	329	34% helix, 22% strand	P02787

Ligands and binding sites

FE · Fe (III) 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

2 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	200	0.71	0.88	39	empty
2	82	0.36	0.76	20	empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

1N7W · Crystal Structure of Human Serum Transferrin, N-Lobe L66W mutant · 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 1N7W · PDBe 1N7W · UniProt P02787

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