Structure of PDB 7esr Chain A

Receptor sequence
>7esrA (length=378) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence]
PPSEAEEALIKETRLPLTGWQQEVDQGLTYGLEAAASIKDRSIPTFSRGE
LPHYAGINTFMKAPYLEDVREVGKYDVAIVGVPHDSGTTYRPGTRFGPQG
IRRISALYTPYNFEMGVDLREQISLCDVGDIFTIPANNEKSFDQISKGIA
HIFSSGAFPIILGGDHSIGFPTVRGICRHLGDKKVGIIHFDRHVDTQETD
LDERMHTCPWFHATNMANAPAKNLVQLGIGGWQVPRQGVKVCRERATNIL
TVTDITEMSLDAAADFAIARATDGTDCVWISFDIDCIDAGFVPGTGWPEP
GGLLPREALYLLKRIIRETNVCGMEVVEVSPPYDISDMTSLMATRVICDT
MAHLVVSGQLPRTEKPAYIHAEANMAVD
3D structure
PDB7esr Discovery of a Ni 2+ -dependent guanidine hydrolase in bacteria.
ChainA
Resolution1.42 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.3.11: agmatinase.
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 CA A D201 H203 D293 D295 D191 H193 D283 D285
BS02 CA A H176 D201 D205 D293 H166 D191 D195 D283
Gene Ontology
Molecular Function
GO:0008783 agmatinase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
Biological Process
GO:0033389 putrescine biosynthetic process from arginine, using agmatinase
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7esr, PDBe:7esr, PDBj:7esr
PDBsum7esr
PubMed35264792
UniProtP73270|GDMH_SYNY3 Guanidine hydrolase (Gene Name=gdmH)

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