MolNFT v1 · #190565 · protein

Crystal structure of the aminopropyltransferase, spee from hyperthermophilic crenarchaeon, pyrobaculum calidifontis in complex with 5'-methylthioadenosine (mta) and spermine

7XIG: “Crystal structure of the aminopropyltransferase, spee from hyperthermophilic crenarchaeon, pyrobaculum…”. X-ray diffraction, 2 ligands (MTA, SPM). MolNFT v1 #190565 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7XIG
Type: protein
Length: 2,294 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: A3MU81
Ligands: MTA, SPM

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, F, G	—	protein	286	—	A3MU81
B, D, H	—	protein	288	—	A3MU81

Ligands and binding sites

MTA · 5'-deoxy-5'-methylthioadenosine · ligand · 8 copies · chains A, B, C, D, E, F, G, H
SPM · Spermine · ligand · 8 copies · chains A, B, C, D, E, F, G, H
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, D, F, G

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

Compared structures

7XIG · Crystal structure of the aminopropyltransferase, SpeE from hyperthermophilic… · the same entry in another collection · chain H against H, TM-score 1.00
A3MU81 · AlphaFold monomer V2.0 prediction for polyamine aminopropyltransferase (A3MU81) · 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 A3MU81
Elsewhere: RCSB PDB 7XIG · PDBe 7XIG · UniProt A3MU81

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