Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5LLN

Crystal structure of human carbonic anhydrase isozyme XIII with 2,3,5,6-Tetrafluoro-4-(propylthio)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 Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS96
BHIS98
BHIS121
BTHR201
B3TV304

site_idAC2
Number of Residues8
Detailsbinding site for residue CIT B 302
ChainResidue
BSER245
BHIS247
BHOH442
BHOH563
AHOH429
BGLY100
BSER101
BHIS105

site_idAC3
Number of Residues11
Detailsbinding site for residue CIT B 303
ChainResidue
ALYS257
BHIS66
BASN69
BARG93
BGLN94
B3TV304
BHOH409
BHOH446
BHOH497
BHOH499
BHOH522

site_idAC4
Number of Residues14
Detailsbinding site for residue 3TV B 304
ChainResidue
BHIS66
BGLN94
BHIS96
BHIS98
BHIS121
BVAL123
BPHE133
BVAL145
BLEU200
BTHR201
BVAL202
BTRP211
BZN301
BCIT303

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS96
AHIS98
AHIS121
A3TV303

site_idAC6
Number of Residues9
Detailsbinding site for residue CIT A 302
ChainResidue
AGLY100
ASER101
AHIS105
ASER245
AHIS247
AHOH470
AHOH494
AHOH540
AHOH618

site_idAC7
Number of Residues12
Detailsbinding site for residue 3TV A 303
ChainResidue
AGLN94
AHIS96
AHIS98
AHIS121
AVAL123
APHE133
ALEU200
ATHR201
AVAL202
ATRP211
AZN301
AHOH686

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon