Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2Q5Q

X-ray structure of phenylpyruvate decarboxylase in complex with 3-deaza-ThDP and 5-phenyl-2-oxo-valeric acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0009851biological_processauxin biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0030976molecular_functionthiamine pyrophosphate binding
A0047434molecular_functionindolepyruvate decarboxylase activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0009851biological_processauxin biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
B0030976molecular_functionthiamine pyrophosphate binding
B0047434molecular_functionindolepyruvate decarboxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 4001
ChainResidue
BASP429
BASN456
BSER458
BTPW2001
BHOH5007

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 4002
ChainResidue
AHOH5009
AASP429
AASN456
ASER458
ATPW2002

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TPW B 2001
ChainResidue
APRO23
AGLY24
AGLU48
AALA74
AKPV5001
BASP382
BALA402
BMET404
BASP429
BGLY430
BALA431
BASN456
BSER458
BTRP459
BGLU460
BMET461
BLEU462
BMG4001
BHOH5007
BHOH5029
BHOH5034
BHOH5199

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE TPW A 2002
ChainResidue
AASP382
AALA402
AMET404
AGLY428
AASP429
AGLY430
AALA431
AASN456
ASER458
ATRP459
AGLU460
AMET461
ALEU462
AMG4002
AHOH5008
AHOH5009
AHOH5086
AHOH5198
BPRO23
BGLY24
BGLU48
BALA74
BKPV5002

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE KPV A 5001
ChainResidue
AGLY24
AASP25
AHIS112
AHIS113
AHOH5010
BASP282
BTHR283
BALA402
BLEU462
BPHE465
BPHE532
BGLN536
BTPW2001

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE KPV B 5002
ChainResidue
AASP282
ATHR283
AALA402
AMET461
ALEU462
APHE465
ATPW2002
BGLY24
BASP25
BHIS112
BHIS113
BHOH5006

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE KPV B 5003
ChainResidue
BARG60
BARG214
BARG215
BMET238
BARG240
BGLY241
BLEU375
BGLY394
BLEU395
BMET396
BALA397
BHOH5394

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE KPV A 5004
ChainResidue
AGLY394
ALEU395
AMET396
AALA397
AHOH5025
AARG60
AARG214
AARG215
AMET238
AARG240
AGLY241
ALEU375

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TLA A 5007
ChainResidue
AASP473
ALEU474
AARG522
AHOH5311
AHOH5536
AHOH5543
AHOH5544
BARG444
BHOH5186

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 5005
ChainResidue
BTHR235
BARG240
BGLY241
BLEU242
BALA244
BASP392
BHOH5173
BHOH5436

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 5006
ChainResidue
ATHR235
AARG240
AGLY241
ALEU242
AALA244
AASP392
AHOH5343
AHOH5394

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues156
DetailsRegion: {"description":"Thiamine pyrophosphate binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon