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Structure of mare apolactoferrin: the N and C lobes are in the closed form

Analyse Structure of mare apolactoferrin: the N and C lobes are in the closed form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B7U
Type: protein
Length: 689 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (apolactoferrin)
UniProt: O77811
Pockets: 12 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (apolactoferrin)	protein	689	34% helix, 15% strand	O77811

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.76	0.98	23	empty
2	97	0.76	0.97	24	empty
3	87	0.75	0.97	24	empty
4	302	0.71	0.84	42	empty
5	483	0.68	0.79	66	empty

Modifications

Observed in the structure: 17 disulfide (disulfide).

Compared structures

1B7U · Structure of Mare Apolactoferrin: the N and C Lobes are in the Closed Form · the same entry in another collection · chain A against A, TM-score 1.00
O77811 · AlphaFold monomer V2.0 prediction for lactotransferrin (O77811) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O77811
Elsewhere: RCSB PDB 1B7U · PDBe 1B7U · UniProt O77811

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