MolNFT v1 · #179110 · protein

Structure of the M101A variant of the sida ornithine hydroxylase complexed with NADP and the FAD in the "out" conformation

7JVL: “Structure of the M101A variant of the sida ornithine hydroxylase complexed with NADP and the FAD in the "out"…”. X-ray diffraction, 3 ligands (FAD, NAP, CA). MolNFT v1 #179110 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7JVL
Type: protein
Length: 1,762 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: E9QYP0
Ligands: FAD, NAP, CA

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	439	—	E9QYP0
B	—	protein	442	—	E9QYP0
C	—	protein	441	—	E9QYP0
D	—	protein	440	—	E9QYP0

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
CA · Calcium ion · metal · 2 copies · chains A, B, C, D
ACT · Acetate ion · additive · 8 copies · chains A, B, C, D

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

Compared structures

7JVL · Structure of the M101A variant of the SidA ornithine hydroxylase complexed with NADP and… · the same entry in another collection · chain D against D, TM-score 1.00
E9QYP0 · AlphaFold monomer V2.0 prediction for L-ornithine N(5)-monooxygenase (E9QYP0) · a predicted model of the same protein · 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 E9QYP0
Elsewhere: RCSB PDB 7JVL · PDBe 7JVL · UniProt E9QYP0

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