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3N2E

Crystal structure of Helicobactor pylori shikimate kinase in complex with NSC162535

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004765molecular_functionshikimate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016301molecular_functionkinase activity
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004765molecular_functionshikimate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016301molecular_functionkinase activity
B0019752biological_processcarboxylic acid metabolic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004765molecular_functionshikimate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008652biological_processamino acid biosynthetic process
C0009073biological_processaromatic amino acid family biosynthetic process
C0009423biological_processchorismate biosynthetic process
C0016301molecular_functionkinase activity
C0019752biological_processcarboxylic acid metabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE OSA A 1001
ChainResidue
APHE9
AMET84
AARG116
AARG132
ALEU135
ATYR136
AHOH179
AHOH201
ATLA2001
ATLA2002
AMET10
AARG45
APHE48
AGLU53
AARG57
AGLY80
AGLY81
AVAL83

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TLA A 2001
ChainResidue
AGLU53
AARG116
ALEU118
AARG132
AHOH184
AOSA1001

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TLA A 2002
ChainResidue
APHE9
APHE101
AILE105
AARG116
ALEU119
AALA125
ALEU128
APHE129
AARG132
AOSA1001

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE OSA B 1001
ChainResidue
BPHE9
BMET10
BARG45
BPHE48
BGLU53
BARG57
BGLY80
BVAL83
BMET84
BARG116
BARG132
BLEU135
BTYR136
BHOH170
BHOH187
BTLA2001
BTLA2003

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TLA B 2001
ChainResidue
BGLU53
BARG116
BARG132
BHOH172
BOSA1001

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TLA B 2002
ChainResidue
BMET10
BGLY11
BSER12
BGLY13
BLYS14
BSER15
BASP31
BHOH198

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TLA B 2003
ChainResidue
BPHE9
BMET10
BLEU104
BILE105
BARG116
BALA125
BLEU128
BARG132
BOSA1001

Functional Information from PROSITE/UniProt
site_idPS01128
Number of Residues27
DetailsSHIKIMATE_KINASE Shikimate kinase signature. RmfEknlIdelktlktph..VIStGGGiV
ChainResidueDetails
AARG57-VAL83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY11
ASER15
AARG116
BGLY11
BSER15
BARG116
CGLY11
CSER15
CARG116

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AASP33
CARG57
CGLY80
CARG132
AARG57
AGLY80
AARG132
BASP33
BARG57
BGLY80
BARG132
CASP33

222036

PDB entries from 2024-07-03

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