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4KNN

Crystal structure of human carbonic anhydrase isozyme XIII with 2-Chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]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 B 301
ChainResidue
BHIS96
BHIS98
BHIS121
BE1F302

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE E1F B 302
ChainResidue
BVAL123
BPHE133
BVAL145
BSER199
BLEU200
BTHR201
BVAL202
BTRP211
BZN301
BHOH467
BHOH601
BHOH623
BHOH644
BARG93
BGLN94
BHIS96
BHIS98
BHIS121

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT B 303
ChainResidue
AHOH466
BGLY100
BSER101
BHIS105
BSER245
BHIS247
BHOH456
BHOH529

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
AARG82
AGLY83
BPRO189
BSER190
BHOH541
BHOH610
BHOH680

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
ATYR42
ASER44
AHIS263
BTYR42
BHIS263

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 306
ChainResidue
BTYR42
BASP43
BLYS257
BARG259
BACY307

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY B 307
ChainResidue
AHOH444
AHOH622
BLYS257
BARG259
BACY306
BHOH498
BHOH607

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY B 308
ChainResidue
AASP104
BGLU76
BHOH548

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS96
AHIS98
AHIS121
AE1F302

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE E1F A 302
ChainResidue
AHIS96
AHIS98
AHIS121
APHE133
AVAL145
ALEU200
ATHR201
AVAL202
ATRP211
AZN301
AHOH589

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT A 303
ChainResidue
AGLY100
ASER101
AHIS105
AGLU154
ASER245
AHIS247
AHOH575
AHOH620

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 304
ChainResidue
AASP28
AGLN29
ALYS254
AARG256
BLYS59
BILE60
BARG177

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
ALYS161
AARG177
APHE178
ATHR179
AHOH476

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV
ChainResidueDetails
BSER107-VAL123

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

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

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

224201

PDB entries from 2024-08-28

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