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Structure of the napb subunit of the periplasmic nitrate reductase from haemophilus influenzae.

Analyse Structure of the napb subunit of the periplasmic nitrate reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JNI
Type: protein
Length: 62 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diheme cytochrome C napb
UniProt: P44654
Ligands: HEC
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diheme cytochrome C napb	protein	62	23% helix, 6% strand	P44654

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	192	0.58	0.80	28	HEC

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

1JNI · Structure of the NapB subunit of the periplasmic nitrate reductase from Haemophilus… · the same entry in another collection · chain A against A, TM-score 1.00
P44654 · AlphaFold monomer V2.0 prediction for periplasmic nitrate reductase, electron transfer… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P44654
Elsewhere: RCSB PDB 1JNI · PDBe 1JNI · UniProt P44654

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