Structure of PDB 1ho3 Chain B

Receptor sequence
>1ho3B (length=326) Species: 562 (Escherichia coli) [Search protein sequence]
LPNITILATGGTIAGGGDSATKSNFTVGKVGVENLVNAVPQLKDIANVKG
EQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD
LTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVM
NDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSD
TPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLY
KSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQ
KARVLLQLALTQTKDPQQIQQIFNQY
3D structure
PDB1ho3 Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T12 F25 T89 D90 K162 E283
Catalytic site (residue number reindexed from 1) T12 F25 T89 D90 K162 E283
Enzyme Commision number 3.5.1.1: asparaginase.
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 ASP B T12 S58 G88 T89 D90 T12 S58 G88 T89 D90
Gene Ontology
Molecular Function
GO:0004067 asparaginase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0006528 asparagine metabolic process
GO:0006530 asparagine catabolic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0032991 protein-containing complex
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ho3, PDBe:1ho3, PDBj:1ho3
PDBsum1ho3
PubMed11223513
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

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