Structure of PDB 6lna Chain B

Receptor sequence
>6lnaB (length=464) Species: 562 (Escherichia coli) [Search protein sequence]
TLSFITRWRDELPATYTTLSPTPLNNARLIWHNAELANTLGIPSSLFKAG
VWGGETLLPGMSPLAQVYSGHQFGVWAGQLGDGRGILLGEQRLADGTTMD
WHLKGAGLTPYSRMGDGRAVLRSTIRESLASEAMHYLGIPTTRALSIVTS
DSPVYRETVEPGAMLMRVAPSHLRFGHFEHFYYRREPEKVRQLADFAIRH
YWSHLADDEDKYRLWFTDVVARTASLIAQWQTVGFAHGVMNTDNMSLLGL
TLDYGPFGFLDDYEPGFISNHSDHQGRYSFDNQPAVALWNLQRLAQTLSP
FVAVDALNEALDSYQQVLLTHYGQRMRQKLGFMTEQKEDNALLNELFSLM
ARERSDYTRTFRMLSLTEQHSAASPLRDEFIDRAAFDDWFARYRGRLQQD
EVSDSERQQLMQSVNPALVLRNWLAQRAIEAAEKGDMTELHRLHEALRNP
FSDRDDDYVSRPPD
3D structure
PDB6lna The YdiU Domain Modulates Bacterial Stress Signaling through Mn 2+ -Dependent UMPylation.
ChainB
Resolution1.701 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.108: protein 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 MN B N247 D256 N244 D253
BS02 ANP B L83 G84 G86 R87 K107 S115 R116 G118 D119 G120 R170 R177 N247 D256 L80 G81 G83 R84 K104 S112 R113 G115 D116 G117 R167 R174 N244 D253
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0070733 AMPylase activity
Biological Process
GO:0018117 protein adenylylation

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Molecular Function

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Biological Process
External links
PDB RCSB:6lna, PDBe:6lna, PDBj:6lna
PDBsum6lna
PubMed32966796
UniProtP77649|SELO_ECOLI Protein adenylyltransferase SelO (Gene Name=selO)

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