Structure of PDB 6eok Chain D Binding Site BS01

Receptor Information

>6eok Chain D (length=302) Species: 83333 (Escherichia coli K-12)

LPNITILATGGTIAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKIN
TDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSAD
GPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSV
NYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANAS
DLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVP
TGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFN
QY

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 6eok Chain D Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6eok Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics.
• Resolution: 2.5 Å
• Binding residue (original residue number in PDB): D100 H197
• Binding residue (residue number reindexed from 1): D76 H173
• Annotation score: 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.

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

External links

• PDB: RCSB:6eok, PDBe:6eok, PDBj:6eok
• PDBsum: 6eok
• PubMed: 30462348
• UniProt: P00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)