Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3PFP

Structure of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis in complex with an active site inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0009423biological_processchorismate biosynthetic process
A0016740molecular_functiontransferase activity
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0051260biological_processprotein homooligomerization
B0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0009423biological_processchorismate biosynthetic process
B0016740molecular_functiontransferase activity
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
B0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 700
ChainResidue
ACYS87
AHIS369
AGLU411
AASP441
A035463
A036716

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 035 A 463
ChainResidue
APRO134
AARG135
ASER136
AGLY282
AGLU283
AARG284
ALYS306
AARG337
AHIS369
ALYS380
AGLU411
ACYS440
AASP441
AHOH469
AHOH473
AHOH491
AHOH503
AHOH556
AHOH681
AMN700
ACYS87
AARG126
ALYS133

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 036 A 716
ChainResidue
ACYS87
AARG126
ALYS133
AARG135
ASER136
AGLY282
AGLU283
AARG284
ALYS306
AARG337
AHIS369
ALYS380
AGLU411
AASP441
AHOH469
AHOH473
AHOH491
AHOH503
AHOH556
AHOH681
AMN700

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 701
ChainResidue
BCYS87
BHIS369
BGLU411
BASP441
B036463
B035771

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 036 B 463
ChainResidue
BCYS87
BARG126
BLYS133
BPRO134
BARG135
BSER136
BGLY282
BGLU283
BARG284
BLYS306
BARG337
BHIS369
BLYS380
BGLU411
BASP441
BHOH488
BHOH592
BHOH597
BHOH606
BHOH634
BHOH670
BMN701
BHOH749

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 464
ChainResidue
BARG435

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 465
ChainResidue
BARG23
BLEU26
BGLU53
BARG256
BHOH489
BHOH647
BHOH663

site_idAC8
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 035 B 771
ChainResidue
BLYS380
BGLU411
BASP441
BHOH488
BHOH592
BHOH597
BHOH606
BHOH634
BHOH670
BMN701
BHOH749
BCYS87
BARG126
BLYS133
BPRO134
BARG135
BSER136
BGLY282
BGLU283
BARG284
BLYS306
BARG337
BHIS369

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:16288916, ECO:0007744|PDB:2B7O
ChainResidueDetails
ACYS87
BARG126
BGLU283
BLYS306
BARG337
BHIS369
BGLU411
BASP441
AARG126
AGLU283
ALYS306
AARG337
AHIS369
AGLU411
AASP441
BCYS87

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon