Research workbench

Kuenenia stuttgartiensis hydrazine synthase

Analyse Kuenenia stuttgartiensis hydrazine synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C2V
Type: protein
Length: 2,877 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q1Q0T2, Q1Q0T4, Q1Q0T3

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	771	—	Q1Q0T2
B, E	—	protein	353	—	Q1Q0T4
C	—	protein	315	—	Q1Q0T3
D	—	protein	771	—	Q1Q0T2
F	—	protein	314	—	Q1Q0T3

Compared structures

5C2V · Kuenenia stuttgartiensis Hydrazine Synthase · the same entry in another collection · chain F against F, TM-score 1.00
Q1Q0T3 · AlphaFold monomer V2.0 prediction for hydrazine synthase subunit gamma (Q1Q0T3) · a predicted model of the same protein · chain F against A, TM-score 1.00
Q1Q0T4 · AlphaFold monomer V2.0 prediction for hydrazine synthase subunit beta (Q1Q0T4) · a predicted model of the same protein · chain B against A, TM-score 0.99
Q1Q0T2 · AlphaFold monomer V2.0 prediction for hydrazine synthase subunit alpha (Q1Q0T2) · a predicted model of the same protein · chain D 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 Q1Q0T2
Every structure of UniProt Q1Q0T4
Every structure of UniProt Q1Q0T3
Elsewhere: RCSB PDB 5C2V · PDBe 5C2V · UniProt Q1Q0T2 · UniProt Q1Q0T4 · UniProt Q1Q0T3

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