Structure of PDB 6eok Chain D

Receptor sequence
>6eokD (length=302) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LPNITILATGGTIAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKIN
TDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSAD
GPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSV
NYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANAS
DLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVP
TGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFN
QY
3D structure
PDB6eok Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics.
ChainD
Resolution2.5 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) T12 T89 D90 K162 E283
Catalytic site (residue number reindexed from 1) T12 T65 D66 K138 E259
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 D D100 H197 D76 H173
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6eok, PDBe:6eok, PDBj:6eok
PDBsum6eok
PubMed30462348
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

[Back to BioLiP]