Structure of PDB 2zy5 Chain D

Receptor sequence
>2zy5D (length=511) Species: 32001 (Alcaligenes faecalis subsp. faecalis) [Search protein sequence]
KIASSDGNRLMLNAGRGNPNFLATTPRRAFFRLGLFAAAESELSYSYMTT
VGVGGLAKIDGIEGRFERYIAENRDQEGVRFLGKSLSYVRDQLGLDPAAF
LHEMVDGILGCNYPVPPRMLNISEKIVRQYIIREMGADAIPSESVNLFAV
EGGTAAMAYIFESLKLNGLLKAGDKVAIGMPVFTPYIEIPELAQYALEEV
AINADPSLNWQYPDSELDKLKDPAIKIFFCVNPSNPPSVKMDQRSLERVR
NIVAEHRPDLMILTDDVYGTFADDFQSLFAICPENTLLVYSFSKYFGATG
WRLGVVAAHQQNVFDLALDKLQESEKVALDHRYRSLLPDVRSLKFIDRLV
ADSRAVALNHTAGLSTPQQVQMALFSLFALMDEADEYKHTLKQLIRRRET
TLYRELGMPPLRDENAVDYYTLIDLQDVTAKLYGEAFSEWAVKQSSTGDM
LFRIADETGIVLLPGAGFGSNRPSGRASLANLNEYEYAAIGRALRKMADE
LYAEYSGQAQN
3D structure
PDB2zy5 Structure, Assembly, and Mechanism of a PLP-Dependent Dodecameric l-Aspartate beta-Decarboxylase
ChainD
Resolution2.65 Å
3D
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
Enzyme Commision number 2.6.1.1: aspartate transaminase.
4.1.1.12: aspartate 4-decarboxylase.
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 PLP D R37 G173 G174 T175 N256 D286 V288 Y289 S312 S314 K315 R323 R16 G152 G153 T154 N235 D265 V267 Y268 S291 S293 K294 R302
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0016831 carboxy-lyase activity
GO:0016847 1-aminocyclopropane-1-carboxylate synthase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0047688 aspartate 4-decarboxylase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006523 alanine biosynthetic process
GO:0006531 aspartate metabolic process
GO:0008652 amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0042218 1-aminocyclopropane-1-carboxylate biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2zy5, PDBe:2zy5, PDBj:2zy5
PDBsum2zy5
PubMed19368885
UniProtQ93QX0|ASDA_COMTE Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase (Gene Name=asD)

[Back to BioLiP]