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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5LL4

Crystal structure of human carbonic anhydrase isozyme II with 4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004064molecular_functionarylesterase activity
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0015670biological_processcarbon dioxide transport
A0016829molecular_functionlyase activity
A0018820molecular_functioncyanamide hydratase activity
A0038166biological_processangiotensin-activated signaling pathway
A0044070biological_processregulation of monoatomic anion transport
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0051453biological_processregulation of intracellular pH
A0070062cellular_componentextracellular exosome
A2001150biological_processpositive regulation of dipeptide transmembrane transport
B0004064molecular_functionarylesterase activity
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008270molecular_functionzinc ion binding
B0015670biological_processcarbon dioxide transport
B0016829molecular_functionlyase activity
B0018820molecular_functioncyanamide hydratase activity
B0038166biological_processangiotensin-activated signaling pathway
B0044070biological_processregulation of monoatomic anion transport
B0045177cellular_componentapical part of cell
B0046872molecular_functionmetal ion binding
B0051453biological_processregulation of intracellular pH
B0070062cellular_componentextracellular exosome
B2001150biological_processpositive regulation of dipeptide transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
A6YH306
site_idAC2
Number of Residues4
Detailsbinding site for residue DMS A 302
ChainResidue
ATYR7
AASP243
ATRP245
AHOH427
site_idAC3
Number of Residues9
Detailsbinding site for residue BCN A 303
ChainResidue
ALYS213
AGLU214
APRO215
AHOH435
AHOH459
AHOH488
AHOH492
AHOH672
ALYS149
site_idAC4
Number of Residues4
Detailsbinding site for residue PEG A 304
ChainResidue
ATRP245
APRO247
AHOH515
AHOH590
site_idAC5
Number of Residues5
Detailsbinding site for residue MLA A 305
ChainResidue
AASN67
AGLN92
APHE131
A6YH306
AHOH631
site_idAC6
Number of Residues13
Detailsbinding site for residue 6YH A 306
ChainResidue
AHIS94
AHIS96
AHIS119
APHE131
ALEU198
ATHR199
ATHR200
APRO202
ATRP209
AZN301
AMLA305
AHOH483
AHOH646
site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
B6YH305
site_idAC8
Number of Residues4
Detailsbinding site for residue DMS B 302
ChainResidue
BTYR7
BASP243
BTRP245
BHOH854
site_idAC9
Number of Residues8
Detailsbinding site for residue BCN B 303
ChainResidue
BLYS149
BLYS213
BGLU214
BPRO215
BHOH665
BHOH669
BHOH724
BHOH779
site_idAD1
Number of Residues6
Detailsbinding site for residue MLA B 304
ChainResidue
BASN67
BILE91
BGLN92
BPHE131
B6YH305
BHOH790
site_idAD2
Number of Residues13
Detailsbinding site for residue 6YH B 305
ChainResidue
BHIS94
BHIS96
BHIS119
BPHE131
BLEU198
BTHR199
BTHR200
BPRO202
BTRP209
BZN301
BMLA304
BHOH635
BHOH827
Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
ChainResidueDetails
ASER105-VAL121
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues512
DetailsDomain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15667203","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4621826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11076507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12499545","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1336460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1433293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1909891","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19583303","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3151020","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7761440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7803386","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7901850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8262987","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8331673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8399159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8431430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8451242","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8482389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8639494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8987974","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9865942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10550681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19520834","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsSite: {"description":"Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Involved in the binding of some activators, including histamine and L-histidine","evidences":[{"source":"PubMed","id":"16214338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9265618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330962","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P27139","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
AHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS94metal ligand
AHIS96metal ligand
AGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS119metal ligand
ATHR199activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity
site_idMCSA2
Number of Residues6
DetailsM-CSA 216
ChainResidueDetails
BHIS64hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS94metal ligand
BHIS96metal ligand
BGLU106activator, electrostatic stabiliser, hydrogen bond acceptor
BHIS119metal ligand
BTHR199activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

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PDB entries from 2026-01-14

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