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

3AHD

Phosphoketolase from Bifidobacterium Breve complexed with 2-acetyl-thiamine diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005975biological_processcarbohydrate metabolic process
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 826
ChainResidue
AASP182
AASN215
ATYR217
AHTL827
AHOH1253

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HTL A 827
ChainResidue
AGLY181
AASP182
AGLY183
AGLU184
AASN215
ATYR217
ALYS218
AILE219
ALYS300
AHIS320
AASP436
AGLU437
ALEU477
AGLU479
ATYR501
APHE504
AASN549
AHIS553
AMG826
AHOH882
AHOH1253
ATHR67
AHIS97
AGLY155
ALEU157

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 828
ChainResidue
AHIS726
AHIS726
AASP727
AASP727

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 829
ChainResidue
ATYR755
APHE780
AGLU797
AHOH1453

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 830
ChainResidue
AGLN11
ALYS12
AASP14
AASN253
AHOH1551

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 831
ChainResidue
AALA220
ATRP317
ALYS452
AVAL463
AASP464
AGLU465
AMET467

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 832
ChainResidue
APHE251
ATHR283
ALYS312
AGLU314

Functional Information from PROSITE/UniProt
site_idPS60002
Number of Residues7
DetailsPHOSPHOKETOLASE_1 Phosphoketolase signature 1. EGGELGY
ChainResidueDetails
AGLU153-TYR159

site_idPS60003
Number of Residues19
DetailsPHOSPHOKETOLASE_2 Phosphoketolase signature 2. GavmNnPslFvpcIiGDGE
ChainResidueDetails
AGLY166-GLU184

237992

PDB entries from 2025-06-25

PDB statisticsPDBj update infoContact PDBjnumon