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5JNA

Crystal structure for the complex of human carbonic anhydrase IV and topiramate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005791cellular_componentrough endoplasmic reticulum
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0015701biological_processbicarbonate transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016829molecular_functionlyase activity
A0030658cellular_componenttransport vesicle membrane
A0030667cellular_componentsecretory granule membrane
A0031526cellular_componentbrush border membrane
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0070062cellular_componentextracellular exosome
A0098552cellular_componentside of membrane
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005791cellular_componentrough endoplasmic reticulum
B0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
B0005794cellular_componentGolgi apparatus
B0005802cellular_componenttrans-Golgi network
B0005886cellular_componentplasma membrane
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0009897cellular_componentexternal side of plasma membrane
B0009986cellular_componentcell surface
B0015701biological_processbicarbonate transport
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016324cellular_componentapical plasma membrane
B0016829molecular_functionlyase activity
B0030658cellular_componenttransport vesicle membrane
B0030667cellular_componentsecretory granule membrane
B0031526cellular_componentbrush border membrane
B0046872molecular_functionmetal ion binding
B0048471cellular_componentperinuclear region of cytoplasm
B0070062cellular_componentextracellular exosome
B0098552cellular_componentside of membrane
C0004089molecular_functioncarbonate dehydratase activity
C0005515molecular_functionprotein binding
C0005791cellular_componentrough endoplasmic reticulum
C0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
C0005794cellular_componentGolgi apparatus
C0005802cellular_componenttrans-Golgi network
C0005886cellular_componentplasma membrane
C0006730biological_processone-carbon metabolic process
C0008270molecular_functionzinc ion binding
C0009897cellular_componentexternal side of plasma membrane
C0009986cellular_componentcell surface
C0015701biological_processbicarbonate transport
C0016020cellular_componentmembrane
C0016323cellular_componentbasolateral plasma membrane
C0016324cellular_componentapical plasma membrane
C0016829molecular_functionlyase activity
C0030658cellular_componenttransport vesicle membrane
C0030667cellular_componentsecretory granule membrane
C0031526cellular_componentbrush border membrane
C0046872molecular_functionmetal ion binding
C0048471cellular_componentperinuclear region of cytoplasm
C0070062cellular_componentextracellular exosome
C0098552cellular_componentside of membrane
D0004089molecular_functioncarbonate dehydratase activity
D0005515molecular_functionprotein binding
D0005791cellular_componentrough endoplasmic reticulum
D0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
D0005794cellular_componentGolgi apparatus
D0005802cellular_componenttrans-Golgi network
D0005886cellular_componentplasma membrane
D0006730biological_processone-carbon metabolic process
D0008270molecular_functionzinc ion binding
D0009897cellular_componentexternal side of plasma membrane
D0009986cellular_componentcell surface
D0015701biological_processbicarbonate transport
D0016020cellular_componentmembrane
D0016323cellular_componentbasolateral plasma membrane
D0016324cellular_componentapical plasma membrane
D0016829molecular_functionlyase activity
D0030658cellular_componenttransport vesicle membrane
D0030667cellular_componentsecretory granule membrane
D0031526cellular_componentbrush border membrane
D0046872molecular_functionmetal ion binding
D0048471cellular_componentperinuclear region of cytoplasm
D0070062cellular_componentextracellular exosome
D0098552cellular_componentside of membrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
ATOR302

site_idAC2
Number of Residues10
Detailsbinding site for residue TOR A 302
ChainResidue
AHIS119
ALEU198
ATHR199
ATHR200
AZN301
AASN62
ASER65
AGLN92
AHIS94
AHIS96

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG27
ALEU195
AARG254
ATHR255
AHOH451
AHOH562
BHOH547

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 304
ChainResidue
AGLY50
ATYR51
AASP52
ALYS53
AHOH516
AHOH533

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL A 305
ChainResidue
APHE48
ASER50
ASER78
AILE79
ASER80
APRO87
CGLN60

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BTOR302

site_idAC7
Number of Residues11
Detailsbinding site for residue TOR B 302
ChainResidue
BASN62
BSER65
BGLN92
BHIS94
BHIS96
BHIS119
BLEU198
BTHR199
BTHR200
BZN301
BHOH514

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 B 303
ChainResidue
BARG27
BLEU195
BARG254
BTHR255
BHOH414
BHOH483

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 B 304
ChainResidue
BGLY50
BTYR51
BASP52
BLYS53
BHOH455

site_idAD1
Number of Residues4
Detailsbinding site for residue ACT B 305
ChainResidue
BLYS15
DGLN158
DGLU162
DHOH559

site_idAD2
Number of Residues7
Detailsbinding site for residue GOL B 306
ChainResidue
BPHE48
BSER50
BSER78
BILE79
BSER80
BPRO87
DGLN60

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS94
CHIS96
CHIS119
CTOR302

site_idAD4
Number of Residues11
Detailsbinding site for residue TOR C 302
ChainResidue
CASN62
CSER65
CGLN92
CHIS94
CHIS96
CHIS119
CLEU198
CTHR199
CTHR200
CZN301
CHOH550

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 C 303
ChainResidue
CARG27
CARG254
CTHR255
CHOH463
CHOH488

site_idAD6
Number of Residues6
Detailsbinding site for residue SO4 C 304
ChainResidue
CGLY50
CTYR51
CASP52
CLYS53
CHOH506
CHOH511

site_idAD7
Number of Residues4
Detailsbinding site for residue ACT C 305
ChainResidue
CASN72
CGLN89
AARG46
AARG189

site_idAD8
Number of Residues9
Detailsbinding site for residue GOL C 306
ChainResidue
CLYS103
CASP243
CVAL245
CPRO247
CHOH441
CHOH453
CHOH485
CHOH507
CHOH548

site_idAD9
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS94
DHIS96
DHIS119
DTOR302

site_idAE1
Number of Residues10
Detailsbinding site for residue TOR D 302
ChainResidue
DASN62
DSER65
DGLN92
DHIS94
DHIS96
DHIS119
DLEU198
DTHR199
DTHR200
DZN301

site_idAE2
Number of Residues5
Detailsbinding site for residue SO4 D 303
ChainResidue
DARG27
DARG254
DTHR255
DHOH505
DHOH529

site_idAE3
Number of Residues7
Detailsbinding site for residue SO4 D 304
ChainResidue
AGLU2
DGLY50
DTYR51
DASP52
DLYS53
DHOH462
DHOH477

site_idAE4
Number of Residues10
Detailsbinding site for residue ACT D 305
ChainResidue
DSER98
DASP99
DLEU100
DPRO101
DALA115
DALA150
DARG220
DILE223
DLEU224
DHOH449

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHsLdgehFamEMHIV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS64
BHIS64
CHIS64
DHIS64

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:8942978
ChainResidueDetails
AHIS94
DHIS94
DHIS96
DHIS119
AHIS96
AHIS119
BHIS94
BHIS96
BHIS119
CHIS94
CHIS96
CHIS119

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR199
BTHR199
CTHR199
DTHR199

site_idSWS_FT_FI4
Number of Residues4
DetailsLIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:7625839
ChainResidueDetails
ASER259
BSER259
CSER259
DSER259

224572

PDB entries from 2024-09-04

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