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5B80

Crystal Structure of Hyperthermophilic Thermotoga maritima L-Ketose-3-Epimerase with Cu2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0006020biological_processinositol metabolic process
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
B0006020biological_processinositol metabolic process
B0016853molecular_functionisomerase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 301
ChainResidue
AGLU149
AASP182
AHIS208
AGLU243

site_idAC2
Number of Residues5
Detailsbinding site for residue 1PG A 302
ChainResidue
AGLY106
ALYS145
AASN175
ATYR205
AARG238

site_idAC3
Number of Residues11
Detailsbinding site for residue 1PG A 303
ChainResidue
AMET1
AGLY34
AGLN36
AGLU125
AGLU128
ALEU129
APHE259
ALYS263
AILE266
AILE267
AHOH573

site_idAC4
Number of Residues5
Detailsbinding site for residue CU B 301
ChainResidue
BGLU149
BASP182
BHIS208
BGLU243
BHOH519

site_idAC5
Number of Residues4
Detailsbinding site for residue 1PG B 302
ChainResidue
ALEU140
BLYS145
BASN175
BARG238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:28258150
ChainResidueDetails
AGLU149
AGLU243
BGLU149
BGLU243

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:28258150, ECO:0007744|PDB:5H1W
ChainResidueDetails
AGLU243
BGLU149
BGLU155
BASP182
BHIS185
BHIS208
BARG214
BGLU243
AGLU149
AGLU155
AASP182
AHIS185
AHIS208
AARG214

218500

PDB entries from 2024-04-17

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