Structure of PDB 1zfn Chain A

Receptor sequence

>1zfnA (length=244) Species: 562 (Escherichia coli)

MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLGTPAALYLAGA
GVGTLVLADDDDVHLSNLQRQILFTTEDIDRPKSQVSQQRLTQLNPDIQL
TALQQRLTGEALKDAVARADVVLDCTDNMATRQEINAACVALNTPLITAS
AVGFGGQLMVLTPPWEQGCYRCLWPDNQEPERNCRTAGVVGPVVGVMGTL
QALEAIKLLSGIETPAGELRLFDGKSSQWRSLALRRASGCPVCG

3D structure

• PDB: 1zfn Structural Analysis of Escherichia Coli ThiF.
• Chain: A
• Resolution: 2.75 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R11 D127
• Catalytic site (residue number reindexed from 1): R11 D127
• Enzyme Commision number: 2.7.7.73: sulfur carrier protein ThiS adenylyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	C169 C172 C240 C243	C169 C172 C240 C243
BS02	ATP	A	I34 G35 G37 G38 D59 R70 Q71 K83 T126 D127 T131	I34 G35 G37 G38 D59 R70 Q71 K83 T126 D127 T131

Gene Ontology

Molecular Function

• GO:0004792 thiosulfate sulfurtransferase activity
• GO:0005524 ATP binding
• GO:0008146 sulfotransferase activity
• GO:0008270 zinc ion binding
• GO:0008641 ubiquitin-like modifier activating enzyme activity
• GO:0016779 nucleotidyltransferase activity
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding
• GO:0070733 AMPylase activity

Biological Process

• GO:0009228 thiamine biosynthetic process
• GO:0009229 thiamine diphosphate biosynthetic process
• GO:0052837 thiazole biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:1902503 adenylyltransferase complex
• GO:1990228 sulfurtransferase complex

External links

• PDB: RCSB:1zfn, PDBe:1zfn, PDBj:1zfn
• PDBsum: 1zfn
• PubMed: 15896804
• UniProt: P30138|THIF_ECOLI Sulfur carrier protein ThiS adenylyltransferase (Gene Name=thiF)