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The crystal structure of the ferredoxin receptor fusa from pectobacterium atrosepticum SCRI1043

Analyse The crystal structure of the ferredoxin receptor fusa from pectobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZGV
Type: protein
Length: 1,618 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferredoxin receptor
UniProt: Q6D8U4
Pockets: 14 · best druggability 0.90

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ferredoxin receptor	protein	809	5% helix, 53% strand	Q6D8U4

Ligands and binding sites

BOG · octyl beta-D-glucopyranoside · additive · 4 copies · chains A, B
LDA · Lauryl dimethylamine-N-oxide · additive · 2 copies · chains A

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

Pockets

14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	929	0.90	0.93	94	empty
2	1055	0.89	0.91	109	empty
3	764	0.83	0.87	112	empty
4	700	0.80	0.85	88	empty
5	846	0.78	0.81	93	empty

Interfaces

1 interface between chains.

A–B · 429 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6D8U4
Elsewhere: RCSB PDB 4ZGV · PDBe 4ZGV · UniProt Q6D8U4

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