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3VAA

1.7 Angstrom Resolution Crystal Structure of Shikimate Kinase from Bacteroides thetaiotaomicron

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide 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
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide 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
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BME A 176
ChainResidue
ACYS83

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 177
ChainResidue
APHE84
ATYR85
AHOH209
AHOH459

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEG A 178
ChainResidue
ALYS14
ATHR15
ATHR16
AARG118
ATYR9
AGLY11
AALA12
AGLY13

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME B 176
ChainResidue
BCYS83
BPHE84
BLYS139
BARG140

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 177
ChainResidue
BGLU38
BHIS41
BHOH262
CGLU174

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 178
ChainResidue
BTYR9
BARG57
BGLY79
BGLY80
BILE120
BARG140
BHOH191
BHOH238

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME C 176
ChainResidue
CCYS83
CPHE84
CLYS139
CARG140

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 177
ChainResidue
CTYR9
CGLY11
CALA12
CGLY13
CLYS14
CTHR15
CHOH193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00109","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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