MolNFT v1 · #158776 · protein

Crystal structure of smt fusion peptidyl-prolyl cis-trans isomerase from burkholderia pseudomallei complexed with SF339

6O49: “Crystal structure of smt fusion peptidyl-prolyl cis-trans isomerase from burkholderia pseudomallei complexed…”. X-ray diffraction, 2 ligands (LL7, CA). MolNFT v1 #158776 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6O49
Type: protein
Length: 380 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q12306, Q3JK38
Ligands: LL7, CA

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	191	—	Q12306, Q3JK38
B	—	protein	189	—	Q12306, Q3JK38

Ligands and binding sites

LL7 · (2~{S})-~{N}-[3-oxidanylidene-3-[(3,4,5-trimethoxyphenyl)amino]propyl]-1-(phenylmethyl) sulfonyl-piperidine-2-carboxamide · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Compared structures

6O49 · Crystal structure of smt fusion peptidyl-prolyl cis-trans isomerase from burkholderia… · the same entry in another collection · chain A against A, TM-score 1.00
Q12306 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein SMT3 (Q12306) · a predicted model of the same protein · chain B against A, TM-score 0.40

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 Q12306
Every structure of UniProt Q3JK38
Elsewhere: RCSB PDB 6O49 · PDBe 6O49 · UniProt Q12306 · UniProt Q3JK38

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