Structure of PDB 1frw Chain A

Receptor sequence
>1frwA (length=185) Species: 562 (Escherichia coli) [Search protein sequence]
NLMTTITGVVLAGGKVDKGLLELNGKPLWQHVADALMTQLSHVVVNANRH
QEIYQASGLKVIEDSLADYPGPLAGMLSVMQQEAGEWFLFCPCDTPYIPP
DLAARLNHQRKDAPVVWVHDGERDHPTIALVNRAIEPLLLEYLQAGERRV
MVFMRLAGGHAVDFSDHKDAFVNVNTPEELARWQE
3D structure
PDB1frw The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis.
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.77: molybdenum cofactor guanylyltransferase.
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 MN A K25 D101 K18 D94
BS02 GTP A L12 A13 G14 G15 K25 N53 D71 G78 P79 G82 P99 D101 L11 A12 G13 G14 K18 N46 D64 G71 P72 G75 P92 D94
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016740 transferase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0061603 molybdenum cofactor guanylyltransferase activity
GO:0070568 guanylyltransferase activity
Biological Process
GO:0006777 Mo-molybdopterin cofactor biosynthetic process
GO:0019720 Mo-molybdopterin cofactor metabolic process
GO:1902758 bis(molybdopterin guanine dinucleotide)molybdenum biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1frw, PDBe:1frw, PDBj:1frw
PDBsum1frw
PubMed10978347
UniProtP32173|MOBA_ECOLI Molybdenum cofactor guanylyltransferase (Gene Name=mobA)

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