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5L6K

Crystal Structure of Human Carbonic Anhydrase II in Complex with a Quinoline Oligoamide Foldamer

This is a non-PDB format compatible entry.
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 Residues3
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 302
ChainResidue
AHOH407
AHOH443
AASN62
AALA65
AASN67
AGLN92
AHIS94
ATHR199

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 303
ChainResidue
AASN67
AGLU69
AGLN92
APHE130
DQUJ307

site_idAC7
Number of Residues2
Detailsbinding site for residue NA A 304
ChainResidue
AASP32
AASP110

site_idAC8
Number of Residues5
Detailsbinding site for residue DMS A 305
ChainResidue
AASN11
AHIS15
ATRP16
ALYS18
AASP19

site_idAC9
Number of Residues3
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL B 302
ChainResidue
BASN62
BHIS64
BASN67
BGLN92
BTHR199
BHOH402
BHOH403
BHOH517

site_idAD4
Number of Residues3
Detailsbinding site for residue GOL B 303
ChainResidue
BASN67
BGLU69
BGLN92

site_idAD6
Number of Residues9
Detailsbinding site for residues QUK A 303 and QVS A 304
ChainResidue
AHIS3
AASP19
APHE20
CQVE306
CQUJ303
CHOH403
CHOH404
BASP129
BLYS132

site_idAD7
Number of Residues5
Detailsbinding site for residues QUK A 303 and QUJ A 315
ChainResidue
AHIS3
CQVS305
CQVE306
CHOH403
BGLY131

site_idAD8
Number of Residues10
Detailsbinding site for residues QVS A 304 and QVE A 305
ChainResidue
ASER2
AHIS3
AASP19
APHE20
CQUK304
CQUJ303
CHOH401
CHOH404
BASP129
BLYS132

site_idAE3
Number of Residues24
Detailsbinding site for residues QUJ B 301 and 6H0 B 306
ChainResidue
APHE130
AGLY131
AGOL303
CQUJ303
AHOH404
FHOH101
BHIS94
BHIS96
BHIS119
BPHE130
BVAL142
BLEU197
BTHR198
BTHR199
BPRO201
BTRP208
BZN301
DQUK308
DQVS309
DQVE310
BGOL302
BGOL303
BHOH455
DHOH402

site_idAE4
Number of Residues10
Detailsbinding site for residues QUJ B 301 and QUK B 307
ChainResidue
APHE130
AGLY131
AGOL303
FHOH101
BSER2
BHIS3
DQVS309
DQVE310
EHOH101
DHOH404

site_idAE6
Number of Residues11
Detailsbinding site for residues QUK B 307 and QVS B 308
ChainResidue
BASP19
BPHE20
DQUJ307
DQVE310
EHOH101
DHOH403
DHOH404
AASP129
ALYS132
BSER2
BHIS3

site_idAE7
Number of Residues11
Detailsbinding site for residues QVS B 308 and QVE B 309
ChainResidue
AASP129
ALYS132
BSER2
BHIS3
BASP19
BPHE20
DQUJ307
DQUK308
DHOH401
DHOH403
DHOH405

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
AASN67
BASN62
BASN67

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P27139
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI9
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

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PDB entries from 2024-09-04

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