Structure of PDB 4dz4 Chain F

Receptor sequence
>4dz4F (length=315) Species: 271848 (Burkholderia thailandensis E264) [Search protein sequence]
TLYGDGAIRRPSVYGSSIENTYAGVLSFMRRNYTRDLDGVDVVVSGVPLD
LATTFRSGARLGPSAVRAASVQLAELNPYPWGFDPFDDLAVIDYGDCWFD
AHHPLSIKPAIVEHARTILQSDARMLTLGGDHYITYPLLIAHAQKYGKPL
SLIHFDAHCDTWADDAPDSLNHGTMFYKAVKDGLIDPKASVQVGIRTWND
DYLGINVLDAAWVHEHGARATLERIESIVGGRPAYLTFDIDCLDPAFAPG
TGTPVAGGLSSAQALAIVRGLGGVNLIGADVVEVAPAYDQSEITAIAAAH
VACDLLCLWRQRKAG
3D structure
PDB4dz4 Combining functional and structural genomics to sample the essential Burkholderia structome.
ChainF
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H135 D159 H161 D163 H175 D242 D244 E286
Catalytic site (residue number reindexed from 1) H132 D156 H158 D160 H172 D239 D241 E283
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 F D159 H161 D242 D244 D156 H158 D239 D241
BS02 MN F H135 D159 D163 D242 H132 D156 D160 D239
BS03 UNK F D163 H175 D160 H172
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

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

[Back to BioLiP]