Structure of PDB 4dz4 Chain B

Receptor sequence
>4dz4B (length=323) Species: 271848 (Burkholderia thailandensis E264) [Search protein sequence]
PGSMNETLYGDGAIRRPSVYGSSIENTYAGVLSFMRRNYTRDLDGVDVVV
SGVPLDLATTFRSGARLGPSAVRAASVQLAELNPYPWGFDPFDDLAVIDY
GDCWFDAHHPLSIKPAIVEHARTILQSDARMLTLGGDHYITYPLLIAHAQ
KYGKPLSLIHFDAHCDTWADDAPDSLNHGTMFYKAVKDGLIDPKASVQVG
IRTWNDDYLGINVLDAAWVHEHGARATLERIESIVGGRPAYLTFDIDCLD
PAFAPGTGTPVAGGLSSAQALAIVRGLGGVNLIGADVVEVAPAYDQSEIT
AIAAAHVACDLLCLWRQRKAGAR
3D structure
PDB4dz4 Combining functional and structural genomics to sample the essential Burkholderia structome.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H135 D159 H161 D163 H175 D242 D244 E286
Catalytic site (residue number reindexed from 1) H138 D162 H164 D166 H178 D245 D247 E289
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 MN B H135 D159 D163 D242 H138 D162 D166 D245
BS02 MN B D159 H161 D242 D244 D162 H164 D245 D247
BS03 UNK B H135 D163 H175 H138 D166 H178
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4dz4, PDBe:4dz4, PDBj:4dz4
PDBsum4dz4
PubMed23382856
UniProtQ2T3W4

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