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4HSO

Crystal structure of S213G variant DAH7PS from Neisseria meningitidis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
A0005737cellular_componentcytoplasm
A0008652biological_processamino acid biosynthetic process
A0009058biological_processbiosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
B0005737cellular_componentcytoplasm
B0008652biological_processamino acid biosynthetic process
B0009058biological_processbiosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
C0005737cellular_componentcytoplasm
C0008652biological_processamino acid biosynthetic process
C0009058biological_processbiosynthetic process
C0009073biological_processaromatic amino acid family biosynthetic process
C0009423biological_processchorismate biosynthetic process
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0003849molecular_function3-deoxy-7-phosphoheptulonate synthase activity
D0005737cellular_componentcytoplasm
D0008652biological_processamino acid biosynthetic process
D0009058biological_processbiosynthetic process
D0009073biological_processaromatic amino acid family biosynthetic process
D0009423biological_processchorismate biosynthetic process
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TYR A 401
ChainResidue
AGLN153
BASP9
ALEU177
AGLY180
ALEU181
ASER182
AGLY213
AVAL214
ALYS216
BASP8

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PEP A 402
ChainResidue
AARG94
ATYR96
ALYS99
AGLU145
AGLY165
AALA166
AARG167
ALYS188
AARG236
AHIS270
AGLU304
AMN403
AHOH501
AHOH564

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 403
ChainResidue
ACYS63
AHIS270
AGLU304
AASP324
APEP402

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TYR B 401
ChainResidue
AASP9
BGLN153
BGLY180
BLEU181
BSER182
BVAL214
BLYS216

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PEP B 402
ChainResidue
BARG94
BTYR96
BLYS99
BALA166
BARG167
BLYS188
BARG236
BHIS270
BGLU304
BMN403
BHOH509
BHOH510
BHOH518

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 403
ChainResidue
BCYS63
BHIS270
BGLU304
BASP324
BPEP402

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TYR C 401
ChainResidue
CGLN153
CALA156
CGLY180
CLEU181
CSER182
CGLY213
CVAL214
CLYS216
DASP9
DHOH519

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PEP C 402
ChainResidue
CARG94
CTYR96
CLYS99
CGLY165
CALA166
CARG167
CLYS188
CARG236
CHIS270
CGLU304
CMN403
CHOH511

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 403
ChainResidue
CCYS63
CHIS270
CGLU304
CASP324
CPEP402

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TYR D 401
ChainResidue
CASP8
CASP9
CILE12
DGLN153
DALA156
DGLY180
DLEU181
DSER182
DGLY213
DVAL214

site_idBC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PEP D 402
ChainResidue
DHIS270
DGLU304
DMN403
DHOH512
DHOH515
DARG94
DTYR96
DLYS99
DGLY165
DALA166
DARG167
DLYS188
DARG236

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN D 403
ChainResidue
DCYS63
DHIS270
DGLU304
DASP324
DPEP402

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PDB entries from 2024-06-26

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