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6QN0

Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
C0004089molecular_functioncarbonate dehydratase activity
C0008270molecular_functionzinc ion binding
D0004089molecular_functioncarbonate dehydratase activity
D0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
AJ8Q302

site_idAC2
Number of Residues13
Detailsbinding site for residue J8Q A 302
ChainResidue
ASER135
AVAL143
ALEU198
ATHR199
ATHR200
ATRP209
AZN301
AHOH500
AGLN92
AHIS94
AHIS96
AHIS119
ASER132

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BJ8Q302

site_idAC4
Number of Residues15
Detailsbinding site for residue J8Q B 302
ChainResidue
BGLN92
BHIS94
BHIS96
BHIS119
BVAL121
BSER132
BSER135
BVAL143
BLEU198
BTHR199
BTHR200
BTRP209
BZN301
BHOH459
BHOH521

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS94
CHIS96
CHIS119
CJ8Q302

site_idAC6
Number of Residues14
Detailsbinding site for residue J8Q C 302
ChainResidue
CGLN92
CHIS94
CHIS96
CHIS119
CSER132
CSER135
CVAL143
CLEU198
CTHR199
CTHR200
CTRP209
CZN301
CHOH491
CHOH603

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS94
DHIS96
DHIS119
DJ8Q302

site_idAC8
Number of Residues13
Detailsbinding site for residue J8Q D 302
ChainResidue
DGLN92
DHIS94
DHIS96
DHIS119
DSER132
DSER135
DVAL143
DLEU198
DTHR199
DTHR200
DPRO201
DTRP209
DZN301

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVsgqhFaaELHIV
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:11493685
ChainResidueDetails
AHIS94
AHIS96
AHIS119
BHIS94
BHIS96
BHIS119
CHIS94
CHIS96
CHIS119
DHIS94
DHIS96
DHIS119

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

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN52
AASN136
BASN52
BASN136
CASN52
CASN136
DASN52
DASN136

221051

PDB entries from 2024-06-12

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