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5E2N

Crystal structure of human carbonic anhydrase isozyme XIII with 3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0043209cellular_componentmyelin sheath
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0043209cellular_componentmyelin sheath
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS96
AHIS98
AHIS121
AV14307

site_idAC2
Number of Residues8
Detailsbinding site for residue PEG A 302
ChainResidue
BLYS59
BILE60
BARG177
AASP28
AGLN29
ALEU253
ALYS254
AARG256

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 303
ChainResidue
ATRP191
AASP192
AHOH406
AHOH427
AHOH438
BPRO48
BHOH440

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 304
ChainResidue
AGLN158
ALYS161
APHE181
AASP182
ASER185

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 305
ChainResidue
ALYS161
AARG177
APHE178
ATHR179
AHOH468

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 306
ChainResidue
AGLY100
ASER101
AHIS105
ASER245
AHIS247
AHOH557

site_idAC7
Number of Residues15
Detailsbinding site for residue V14 A 307
ChainResidue
ASER64
AHIS66
ASER67
AASN69
AGLN94
AHIS96
AHIS98
AHIS121
AVAL123
APHE133
ALEU200
ATHR201
AVAL202
AZN301
AHOH474

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS96
BHIS98
BHIS121
BV14306

site_idAC9
Number of Residues9
Detailsbinding site for residue CIT B 302
ChainResidue
AHOH492
BGLY100
BSER101
BHIS105
BSER245
BHIS247
BHOH408
BHOH524
BHOH572

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO B 303
ChainResidue
ASER50
AARG82
BPRO189

site_idAD2
Number of Residues6
Detailsbinding site for residue EDO B 304
ChainResidue
AGLU39
BPRO131
BSER132
BHOH425
BHOH570
BHOH575

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO B 305
ChainResidue
BASP54
BSER56
BLYS78

site_idAD4
Number of Residues18
Detailsbinding site for residue V14 B 306
ChainResidue
BTRP7
BSER64
BHIS66
BSER67
BASN69
BGLN94
BHIS96
BHIS98
BHIS121
BVAL123
BPHE133
BLEU200
BTHR201
BVAL202
BTRP211
BZN301
BHOH500
BHOH571

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV
ChainResidueDetails
ASER107-VAL123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS66
BHIS66

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18618712
ChainResidueDetails
AHIS96
AHIS98
AHIS121
BHIS96
BHIS98
BHIS121

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR201
BTHR201

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PDB entries from 2024-07-24

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