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4MTY

Structure at 1A resolution of a helical aromatic foldamer-protein complex.

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
ASBW302

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE SBW A 302
ChainResidue
ATHR198
ATHR199
APRO201
ATRP208
AZN301
AGOL308
ASBW310
AHOH431
AHOH684
AHOH745
AHIS94
AHIS96
AHIS119
APHE130
ALEU197

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SBW A 303
ChainResidue
AHIS3
ATRP5
AHIS10
AASN11
AHIS15
ATRP16
AASP19
APHE20
AARG181
AGLY182
AHOH575
AHOH787

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HGB A 304
ChainResidue
AGLN135
AGLN136
APRO137
AGLU204
ACYS205
AHG309
AHOH531
AHOH637
AHOH642
AHOH706

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 305
ChainResidue
AASN62
AHIS64
AALA65
AASN67
AGLN92
AHIS94
AHOH416
AHOH568
AHOH612

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
ALYS39
AGLN254
ALYS256
AHOH660

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
ATYR7
APRO13
AASP242
ATRP244
AHOH535
AHOH616
AHOH789

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 308
ChainResidue
AGLN92
APHE130
ASBW302
ASBW310
AHOH721

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 309
ChainResidue
AVAL134
AGLN136
ACYS205
AHGB304
AHOH531

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SBW A 310
ChainResidue
ALEU57
APHE70
AASP72
AILE91
ASBW302
AGOL308
AHOH434
AHOH443
AHOH469
AHOH594
AHOH721

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 Residues256
DetailsDomain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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 Residues1
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 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":"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 Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10550681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19520834","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
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 Residues2
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 Residues1
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":"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
ATHR198activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity

247536

PDB entries from 2026-01-14

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