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

1ZNC

HUMAN CARBONIC ANHYDRASE IV

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
ALEU198
ATHR199
ATRP209
AZN301

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
ATHR199
ASO4601

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS94
BHIS96
BHIS119
BTHR199
BSO4701

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 701
ChainResidue
BHIS119
BLEU198
BTHR199
BTRP209
BZN302

site_idCTA
Number of Residues5
DetailsZINC COORDINATED BY HIS A 94, HIS A 96, AND HIS A 119. ALSO COORDINATED BY AN OXYGEN ON THE SULFATE GROUP.
ChainResidue
AHIS94
AHIS96
AHIS119
AZN301
ASO4601

site_idCTB
Number of Residues5
DetailsZINC COORDINATED BY HIS B 94, HIS B 96, AND HIS B 119. ALSO COORDINATED BY AN OXYGEN ON THE SULFATE GROUP.
ChainResidue
BSO4701
BHIS94
BHIS96
BHIS119
BZN302

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS64
BHIS64

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8942978
ChainResidueDetails
AHIS94
AHIS96
AHIS119
BHIS94
BHIS96
BHIS119

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR199
BTHR199

site_idSWS_FT_FI4
Number of Residues2
DetailsLIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:7625839
ChainResidueDetails
ASER259
BSER259

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
AHIS64

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR199
BHIS64

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon