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1N8F

Crystal structure of E24Q mutant of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (DAHP synthase) from Escherichia Coli in complex with Mn2+ and PEP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
B0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009058biological_processbiosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016740molecular_functiontransferase activity
B0042802molecular_functionidentical protein binding
C0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008652biological_processamino acid biosynthetic process
C0009058biological_processbiosynthetic process
C0009073biological_processaromatic amino acid family biosynthetic process
C0009423biological_processchorismate biosynthetic process
C0016740molecular_functiontransferase activity
C0042802molecular_functionidentical protein binding
D0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008652biological_processamino acid biosynthetic process
D0009058biological_processbiosynthetic process
D0009073biological_processaromatic amino acid family biosynthetic process
D0009423biological_processchorismate biosynthetic process
D0016740molecular_functiontransferase activity
D0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 351
ChainResidue
ACYS61
AHIS268
AGLU302
AASP326
APEP1396
AHOH5416

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 351
ChainResidue
BASP326
BPEP1397
BHOH2376
BCYS61
BHIS268
BGLU302

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 351
ChainResidue
CCYS61
CHIS268
CGLU302
CASP326
CPEP1398
CHOH3451

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN D 351
ChainResidue
DCYS61
DHIS268
DGLU302
DASP326
DPEP1399
DHOH4414

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 5353
ChainResidue
AARG99
ATHR100
AHOH5446

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 2353
ChainResidue
BARG99
BTHR100
BHOH2404
BHOH2433
BHOH2557
BHOH2672

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 3353
ChainResidue
CARG99
CTHR100
CHOH3480
CHOH3509
CHOH3552

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 4353
ChainResidue
DARG99
DTHR100
DHOH4444
DHOH4474
DHOH4547
DHOH4628

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 5356
ChainResidue
ATHR192
AILE193
ALYS194
AHOH5370
AHOH5553
AHOH5587
AHOH5654

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 2356
ChainResidue
BTHR192
BILE193
BLYS194
BHOH2467
BHOH2591
BHOH2641

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 3356
ChainResidue
CTHR192
CILE193
CLYS194
CHOH3405
CHOH3544
CHOH3575

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 4356
ChainResidue
DTHR192
DILE193
DLYS194

site_idBC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PEP A 1396
ChainResidue
AARG92
ALYS97
APRO98
AGLU143
AGLY163
AALA164
AARG165
ALYS186
AARG234
AHIS268
AMN351
AHOH5406
AHOH5413
AHOH5416
AHOH5432
AHOH5461

site_idBC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PEP B 1397
ChainResidue
BARG92
BLYS97
BGLU143
BGLY163
BALA164
BARG165
BLYS186
BARG234
BHIS268
BMN351
BHOH2366
BHOH2373
BHOH2376
BHOH2391
BHOH2419

site_idBC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PEP C 1398
ChainResidue
CGLU143
CGLY163
CALA164
CARG165
CLYS186
CARG234
CHIS268
CGLU302
CMN351
CHOH3441
CHOH3448
CHOH3451
CHOH3467
CHOH3495
CARG92
CLYS97

site_idBC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PEP D 1399
ChainResidue
DARG92
DLYS97
DGLU143
DGLY163
DALA164
DARG165
DLYS186
DARG234
DHIS268
DMN351
DHOH4404
DHOH4411
DHOH4414
DHOH4431
DHOH4460

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS244
BLYS244
CLYS244
DLYS244

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1q3n
ChainResidueDetails
AHIS268

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1q3n
ChainResidueDetails
BHIS268

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1q3n
ChainResidueDetails
CHIS268

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1q3n
ChainResidueDetails
DHIS268

238268

PDB entries from 2025-07-02

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