Structure of PDB 1jwb Chain B

Receptor sequence
>1jwbB (length=240) Species: 562 (Escherichia coli) [Search protein sequence]
AELSDQEMLRYNRQIILRGFDFDGQEALKDSRVLIVGLGGLGCAASQYLA
SAGVGNLTLLDFDTVSLSNLQRQTLHSDATVGQPKVESARDALTRINPHI
AITPVNALLDDAELAALIAEHDLVLDCTDNVAVRNQLNAGCFAAKVPLVS
GAAIRMEGQITVFTYQDGEPCYRCLSRLFGEAGVMAPLIGVIGSLQAMEA
IKMLAGYGKPASGKIVMYDAMTCQFREMKLMRNPGCEVCG
3D structure
PDB1jwb Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R14 D130
Catalytic site (residue number reindexed from 1) R13 D129
Enzyme Commision number 2.7.7.80: molybdopterin-synthase 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 C172 C244 C247 C171 C236 C239
BS02 AMP B G38 G40 G41 D62 F63 K86 L109 C128 T129 D130 N131 V134 G37 G39 G40 D61 F62 K85 L108 C127 T128 D129 N130 V133
Gene Ontology
Molecular Function
GO:0004792 thiosulfate sulfurtransferase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008146 sulfotransferase activity
GO:0008641 ubiquitin-like modifier activating enzyme activity
GO:0016779 nucleotidyltransferase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0061605 molybdopterin-synthase adenylyltransferase activity
Biological Process
GO:0006777 Mo-molybdopterin cofactor biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:1990133 molybdopterin adenylyltransferase complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:1jwb, PDBe:1jwb, PDBj:1jwb
PDBsum1jwb
PubMed11713534
UniProtP12282|MOEB_ECOLI Molybdopterin-synthase adenylyltransferase (Gene Name=moeB)

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