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4HU1

Crystal structure of human carbonic anhydrase isozyme XIII with the inhibitor.

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
BV13302

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE V13 B 302
ChainResidue
BPHE133
BVAL145
BLEU200
BTHR201
BVAL202
BZN301
BHOH475
BHOH542
BGLN94
BHIS96
BHIS98
BHIS121
BVAL123

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
BGLY100
BSER101
BHIS105
BSER245
BHIS247

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BARG10
BGLU11
BHIS12
BASN13

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS96
AHIS98
AHIS121
AV13302

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE V13 A 302
ChainResidue
AGLN94
AHIS96
AHIS98
AHIS121
AVAL123
APHE133
AVAL145
ALEU200
ATHR201
AVAL202
ATRP211
AZN301
AHOH464
AHOH542
AHOH593

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEG A 303
ChainResidue
ALYS59
AILE60
AARG177
BASP28
BGLN29
BLEU253
BLYS254
BARG256

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
APRO189
ASER190
BARG82

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
ALYS38
AGLN160
AGLN223
ALYS227
AHOH425
AHOH645

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AASP54
ASER56

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
AGLY100
ASER101
AHIS105
ASER245
AHIS247
AHOH414
AHOH693

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 308
ChainResidue
AASP103
AILE152
BTHR75
BHOH638
BHOH639

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

221051

PDB entries from 2024-06-12

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