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3FDD

The Crystal Structure of the Pseudomonas dacunhae Aspartate-Beta-Decarboxylase Reveals a Novel Oligomeric Assembly for a Pyridoxal-5-Phosphate Dependent Enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006531biological_processaspartate metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0047688molecular_functionaspartate 4-decarboxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 534
ChainResidue
AARG37
AASP286
ATYR289
ASER312
ASER314
ALYS315
AARG323
ATYR134
AGLY173
AGLY174
ATHR175
APHE204
ATYR207
AVAL252
AASN256

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 535
ChainResidue
AASN41
ASER65
ASER67
AGLN113
AASN504
AHOH584

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 536
ChainResidue
AARG49
AARG53
AGLY99

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKyfGAtGWRLG
ChainResidueDetails
ASER312-GLY325

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APHE204
AASP286
ALYS315

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PDB entries from 2024-07-24

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