Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5KU6

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

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 Residues10
Detailsbinding site for residue MZM A 301
ChainResidue
AGLN92
AHOH473
AHIS94
AHIS96
AHIS119
ALEU198
ATHR199
ATHR200
ATRP209
AZN302

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AHIS94
AHIS96
AHIS119
AMZM301

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG27
ALEU195
AARG254
ATHR255
AHOH455
AHOH568
BHOH539

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 304
ChainResidue
AGLY50
ATYR51
AASP52
ALYS53
AHOH491

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 305
ChainResidue
ASER50
ASER78
AILE79
ASER80
APRO87
CGLN60

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL B 301
ChainResidue
BASN62
BGLN92
BHIS94
BMZM302
BHOH407

site_idAC7
Number of Residues11
Detailsbinding site for residue MZM B 302
ChainResidue
BGLN92
BHIS94
BHIS96
BHIS119
BVAL121
BLEU198
BTHR199
BTHR200
BGOL301
BZN303
BHOH473

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 303
ChainResidue
BHIS94
BHIS96
BHIS119
BMZM302

site_idAC9
Number of Residues6
Detailsbinding site for residue SO4 B 304
ChainResidue
BARG27
BLEU195
BARG254
BTHR255
BHOH447
BHOH468

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 B 305
ChainResidue
BGLY50
BTYR51
BASP52
BLYS53

site_idAD2
Number of Residues4
Detailsbinding site for residue ACT B 306
ChainResidue
BLYS15
DGLU155
DGLN158
DGLU162

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL B 307
ChainResidue
BPHE48
BSER78
BILE79
BSER80
BPRO87
BHOH505
DGLN60
DMET67

site_idAD4
Number of Residues12
Detailsbinding site for residue MZM C 301
ChainResidue
CGLN92
CHIS94
CHIS96
CHIS119
CLEU198
CTHR199
CTHR200
CZN302
CHOH418
CHOH550
CHOH585
CHOH612

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN C 302
ChainResidue
CHIS94
CHIS96
CHIS119
CMZM301

site_idAD6
Number of Residues6
Detailsbinding site for residue SO4 C 303
ChainResidue
CARG27
CARG254
CTHR255
CHOH432
CHOH442
CHOH551

site_idAD7
Number of Residues7
Detailsbinding site for residue SO4 C 304
ChainResidue
CLYS53
CHOH496
CHOH526
CHOH568
CGLY50
CTYR51
CASP52

site_idAD8
Number of Residues4
Detailsbinding site for residue ACT C 305
ChainResidue
AARG46
AARG189
CASN72
CGLN89

site_idAD9
Number of Residues8
Detailsbinding site for residue GOL C 306
ChainResidue
CLYS103
CASP243
CVAL245
CPRO247
CHOH438
CHOH483
CHOH515
CHOH524

site_idAE1
Number of Residues3
Detailsbinding site for residue GOL C 307
ChainResidue
CSER50
CASN72
CSER78

site_idAE2
Number of Residues12
Detailsbinding site for residue MZM D 301
ChainResidue
DGLN92
DHIS94
DHIS96
DHIS119
DVAL121
DLEU198
DTHR199
DTHR200
DTRP209
DZN302
DHOH401
DHOH595

site_idAE3
Number of Residues4
Detailsbinding site for residue ZN D 302
ChainResidue
DHIS94
DHIS96
DHIS119
DMZM301

site_idAE4
Number of Residues6
Detailsbinding site for residue SO4 D 303
ChainResidue
DARG27
DLEU195
DARG254
DTHR255
DHOH424
DHOH448

site_idAE5
Number of Residues6
Detailsbinding site for residue SO4 D 304
ChainResidue
AGLU2
DGLY50
DTYR51
DASP52
DLYS53
DHOH472

site_idAE6
Number of Residues8
Detailsbinding site for residue ACT D 305
ChainResidue
DASP99
DLEU100
DPRO101
DALA115
DALA150
DILE223
DLEU224
DHOH452

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

PDB statisticsPDBj update infoContact PDBjnumon