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Selenium-free nitrogenase Fe protein (Av2) from A. vinelandii (nucleotide control)

Analyse Selenium-free nitrogenase Fe protein (Av2) from A. vinelandii (nucleotide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TPZ
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.71
Source: Azotobacter vinelandii
Molecule: Nitrogenase iron protein 1
EC: 1.18.6.1
UniProt: P00459
Ligands: SF4, ADP, MG
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · resolution 1.71 · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitrogenase iron protein 1 (EC 1.18.6.1)	protein	272	44% helix, 16% strand	P00459

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · chains A
ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	120	0.45	0.78	24	MG, ADP

Compared structures

P00459 · AlphaFold monomer V2.0 prediction for nitrogenase iron protein 1 (P00459) · 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 P00459
Elsewhere: RCSB PDB 7TPZ · PDBe 7TPZ · UniProt P00459

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