Structure of PDB 6eok Chain C

Receptor sequence
>6eokC (length=305) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LPNITILATGGTIAVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAK
KINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSM
SADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATF
KSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYA
NASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSS
RVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQ
IFNQY
3D structure
PDB6eok Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics.
ChainC
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 T89 D90 K162 E283
Catalytic site (residue number reindexed from 1) T12 T68 D69 K141 E262
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 ZN C D100 H197 D79 H176
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:6eok, PDBe:6eok, PDBj:6eok
PDBsum6eok
PubMed30462348
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

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