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5OGN

Metalacarborane inhibitors of Carbonic Anhydrase IX

Functional Information from GO Data
ChainGOidnamespacecontents
A0002009biological_processmorphogenesis of an epithelium
A0004064molecular_functionarylesterase activity
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0015670biological_processcarbon dioxide transport
A0016829molecular_functionlyase activity
A0018820molecular_functioncyanamide hydratase activity
A0032230biological_processpositive regulation of synaptic transmission, GABAergic
A0032849biological_processpositive regulation of cellular pH reduction
A0038166biological_processangiotensin-activated signaling pathway
A0043209cellular_componentmyelin sheath
A0044070biological_processregulation of monoatomic anion transport
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0046903biological_processsecretion
A0051453biological_processregulation of intracellular pH
A0070050biological_processneuron cellular homeostasis
A0070062cellular_componentextracellular exosome
A2001150biological_processpositive regulation of dipeptide transmembrane transport
A2001225biological_processregulation of chloride transport
B0002009biological_processmorphogenesis of an epithelium
B0004064molecular_functionarylesterase activity
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0015670biological_processcarbon dioxide transport
B0016829molecular_functionlyase activity
B0018820molecular_functioncyanamide hydratase activity
B0032230biological_processpositive regulation of synaptic transmission, GABAergic
B0032849biological_processpositive regulation of cellular pH reduction
B0038166biological_processangiotensin-activated signaling pathway
B0043209cellular_componentmyelin sheath
B0044070biological_processregulation of monoatomic anion transport
B0045177cellular_componentapical part of cell
B0046872molecular_functionmetal ion binding
B0046903biological_processsecretion
B0051453biological_processregulation of intracellular pH
B0070050biological_processneuron cellular homeostasis
B0070062cellular_componentextracellular exosome
B2001150biological_processpositive regulation of dipeptide transmembrane transport
B2001225biological_processregulation of chloride transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
AB8B302

site_idAC2
Number of Residues12
Detailsbinding site for residue B8B A 302
ChainResidue
AHIS119
ALEU197
ATHR198
ATHR199
APRO200
AZN301
AHOH541
AHIS3
AHIS64
AGLN92
AHIS94
AHIS96

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS2
AHOH498
BHIS4
BHIS64

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BB8B302

site_idAC5
Number of Residues12
Detailsbinding site for residue B8B B 302
ChainResidue
AHIS2
AHIS3
AHIS4
BGLN92
BHIS94
BHIS96
BHIS119
BLEU197
BTHR198
BTHR199
BPRO200
BZN301

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
ChainResidueDetails
AHIS64
BHIS64

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
ChainResidueDetails
AHIS94
BHIS94

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
ChainResidueDetails
AHIS96
AHIS119
BHIS96
BHIS119

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
ChainResidueDetails
ATHR198
BTHR198

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
ChainResidueDetails
ATYR7
BTYR7

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
ChainResidueDetails
AASN62
AGLN67
BASN62
BGLN67

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
ChainResidueDetails
AGLN92
BGLN92

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER165
ASER172
BSER165
BSER172

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
ATHR198activator, 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
BTHR198activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

225158

PDB entries from 2024-09-18

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