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Ferric binding protein in apo form 1

Analyse Ferric binding protein in apo form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ELO
Type: protein
Length: 1,848 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Iron ABC transporter, periplasmic iron-binding protein
UniProt: Q5SHV2
Pockets: 20 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Iron ABC transporter, periplasmic iron-binding protein	protein	308	47% helix, 17% strand	Q5SHV2

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	763	0.68	0.75	80	empty
2	355	0.62	0.78	49	empty
3	376	0.62	0.77	52	empty
4	353	0.61	0.78	49	empty
5	338	0.59	0.77	55	empty

Interfaces

6 interfaces between chains.

C–D · 1025 Å² buried · 15 hydrogen bonds · protein-protein
B–F · 1011 Å² buried · 14 hydrogen bonds · protein-protein
A–E · 994 Å² buried · 17 hydrogen bonds · protein-protein
A–C · 393 Å² buried · 7 hydrogen bonds · protein-protein
D–F · 296 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4ELO · Ferric binding protein in apo form 1 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q5SHV2
Elsewhere: RCSB PDB 4ELO · PDBe 4ELO · UniProt Q5SHV2

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