Structure of PDB 1frw Chain A Binding Site BS01

Receptor Information

>1frw Chain A (length=185) Species: 562 (Escherichia coli)

NLMTTITGVVLAGGKVDKGLLELNGKPLWQHVADALMTQLSHVVVNANRH
QEIYQASGLKVIEDSLADYPGPLAGMLSVMQQEAGEWFLFCPCDTPYIPP
DLAARLNHQRKDAPVVWVHDGERDHPTIALVNRAIEPLLLEYLQAGERRV
MVFMRLAGGHAVDFSDHKDAFVNVNTPEELARWQE

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 1frw Chain A Residue 197

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1frw The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis.
• Resolution: 1.75 Å
• Binding residue (original residue number in PDB): K25 D101
• Binding residue (residue number reindexed from 1): K18 D94
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.7.7.77: molybdenum cofactor guanylyltransferase.

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

External links

• PDB: RCSB:1frw, PDBe:1frw, PDBj:1frw
• PDBsum: 1frw
• PubMed: 10978347
• UniProt: P32173|MOBA_ECOLI Molybdenum cofactor guanylyltransferase (Gene Name=mobA)