Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5LLP

Crystal structure of human carbonic anhydrase isozyme XII with 3-[(1S)-1,2,3,4-Tetrahydronapthalen-1-ylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]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
AHIS91
AHIS93
AHIS117
A6Z9302

site_idAC2
Number of Residues16
Detailsbinding site for residue 6Z9 A 302
ChainResidue
AHIS93
AGLU104
AHIS117
AALA129
ASER133
ALEU197
ATHR198
ATHR199
APRO200
AZN301
AHOH623
ATRP4
AASN64
ALYS69
AGLN89
AHIS91

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS91
BHIS93
BHIS117
B6Z9302

site_idAC4
Number of Residues12
Detailsbinding site for residue 6Z9 B 302
ChainResidue
BASN64
BSER67
BHIS91
BHIS93
BHIS117
BALA129
BLEU197
BTHR198
BTHR199
BPRO200
BZN301
BHOH439

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN C 301
ChainResidue
CHIS91
CHIS93
CHIS117
C6Z9302

site_idAC6
Number of Residues13
Detailsbinding site for residue 6Z9 C 302
ChainResidue
CASN64
CLYS69
CGLN89
CHIS91
CHIS93
CGLU104
CHIS117
CALA129
CLEU197
CTHR198
CTHR199
CPRO201
CZN301

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN D 301
ChainResidue
DHIS91
DHIS93
DHIS117
D6Z9302

site_idAC8
Number of Residues14
Detailsbinding site for residue 6Z9 D 302
ChainResidue
DASN64
DHIS91
DHIS93
DHIS117
DVAL119
DALA129
DSER130
DLEU197
DTHR198
DTHR199
DPRO200
DZN301
DHOH406
DHOH513

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVsgqhFaaELHIV
ChainResidueDetails
ASER103-VAL119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11493685","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon