Structure of PDB 6pa4 Chain B

Receptor sequence
>6pa4B (length=308) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LPNITILATGGTIVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLT
LAKKINTDCDKTDGFVITHGVDTMEETAYFLDLTVKCDKPVVMVGAMRPS
TSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTTTNTTDV
ATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVY
NYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVV
RSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQ
IQQIFNQY
3D structure
PDB6pa4 Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase.
ChainB
Resolution1.85 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 V89 D90 T162 E283
Catalytic site (residue number reindexed from 1) T12 V71 D72 T144 E265
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 V89 D90 T12 S40 G70 V71 D72
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:6pa4, PDBe:6pa4, PDBj:6pa4
PDBsum6pa4
PubMed31423681
UniProtP00805|ASPG2_ECOLI L-asparaginase 2 (Gene Name=ansB)

[Back to BioLiP]