Structure of PDB 3fdd Chain A

Receptor sequence

>3fddA (length=502) Species: 207291 ([Pseudomonas] dacunhae ATCC 21192)

DGNRLMLNAGRGNPNFLATTPRRAFFRLGLFAAAESELSYSYMNTVGVGG
LAKIEGIEGRFERYIAENRDQEGVRFLGKSLSYVRDQLGLDPAAFLHEMV
DGILGCNYPVPPRMLNISEKIVRQYIIREMGADAIPSESVNLFAVEGGTA
AMAYIFESMKVNGLLKAGDKVAIGMPVFTPYIEIPELAQYALEEVAINAD
PALNWQYPDSELDKLKDPAIKIFFCVNPSNPPSVKMDERSLERVRKIVAE
HRPDLMILTDDVYGTFADGFQSLFAICPANTLLVYSFSKYFGATGWRLGV
VAAHKENIFDLALGRLPESEKTALDDRYRSLLPDVRSLKFLDRLVADSRA
VALNHTAGLSTPQQVQMTLFSLFALMDESDQYKHTLKQLIRRREATLYRE
LGTPPQRDENAVDYYTLIDLQDVTSKLYGEAFSKWAVKQSSTGDMLFRIA
DETGIVLLPGRGFGSDRPSGRASLANLNEYEYAAIGRALRQMADELYAQY
TQ

3D structure

• PDB: 3fdd The crystal structure of the Pseudomonas dacunhae aspartate-beta-decarboxylase dodecamer reveals an unknown oligomeric assembly for a pyridoxal-5'-phosphate-dependent enzyme.
• Chain: A
• Resolution: 2.35 Å

Enzymatic activity

• Enzyme Commision number: 2.6.1.-

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	A	R37 G173 G174 T175 F204 V252 D286 V288 Y289 S312 S314 K315 R323	R11 G147 G148 T149 F178 V226 D260 V262 Y263 S286 S288 K289 R297

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0008483 transaminase activity
• GO:0016847 1-aminocyclopropane-1-carboxylate synthase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0047688 aspartate 4-decarboxylase activity

Biological Process

• GO:0006520 amino acid metabolic process
• GO:0006531 aspartate metabolic process
• GO:0009058 biosynthetic process
• GO:0042218 1-aminocyclopropane-1-carboxylate biosynthetic process

External links

• PDB: RCSB:3fdd, PDBe:3fdd, PDBj:3fdd
• PDBsum: 3fdd
• PubMed: 19265705
• UniProt: Q845W8