Structure of PDB 1zfn Chain B

Receptor sequence
>1zfnB (length=232) Species: 562 (Escherichia coli) [Search protein sequence]
MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLGTPAALYLAGA
GVGTLVLADDDDVHLSNLQRQILFTTEDIDRPKSQVSQQRLTQLNPDIQL
TALQQRLTGEALKDAVARADVVLDCTDNMATRQEINAACVALNTPLITAS
AVGFGGQLMVLTPPWEQGCYRCLWAGVVGPVVGVMGTLQALEAIKLLSGI
ETPAGELRLFDGKSSQWRSLALRRASGCPVCG
3D structure
PDB1zfn Structural Analysis of Escherichia Coli ThiF.
ChainB
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B C169 C172 C169 C172
BS02 ATP B G35 G37 D59 R70 Q71 K83 R106 T126 T131 G35 G37 D59 R70 Q71 K83 R106 T126 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

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Molecular Function
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Cellular Component
External links
PDB RCSB:1zfn, PDBe:1zfn, PDBj:1zfn
PDBsum1zfn
PubMed15896804
UniProtP30138|THIF_ECOLI Sulfur carrier protein ThiS adenylyltransferase (Gene Name=thiF)

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