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

5B7Z

Crystal Structure of Hyperthermophilic Thermotoga maritima L-Ketose-3-Epimerase with Ni2+

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 Residues6
Detailsbinding site for residue MPD A 301
ChainResidue
AARG117
AARG153
ATHR156
AASP157
AHOH451
AHOH549

site_idAC2
Number of Residues6
Detailsbinding site for residue MPD A 302
ChainResidue
AMET104
AHOH416
B1PG304
ALYS97
AGLU100
AVAL101

site_idAC3
Number of Residues4
Detailsbinding site for residue MPD A 303
ChainResidue
AARG214
ACYS244
ALEU245
AHOH480

site_idAC4
Number of Residues4
Detailsbinding site for residue MPD A 304
ChainResidue
ALYS89
AILE92
AARG136
B1PG303

site_idAC5
Number of Residues5
Detailsbinding site for residue NI A 305
ChainResidue
AGLU149
AASP182
AHIS208
AGLU243
AHOH429

site_idAC6
Number of Residues5
Detailsbinding site for residue 1PG A 306
ChainResidue
ALEU108
ALYS145
AASN175
ATYR205
AARG238

site_idAC7
Number of Residues10
Detailsbinding site for residue 1PG A 307
ChainResidue
AMET1
AGLY34
AGLN36
AGLU125
AGLU128
ALEU129
APHE259
ALYS263
AILE266
AILE267

site_idAC8
Number of Residues3
Detailsbinding site for residue MPD B 301
ChainResidue
BARG214
BGLU243
BHOH654

site_idAC9
Number of Residues5
Detailsbinding site for residue NI B 302
ChainResidue
BGLU149
BASP182
BHIS208
BGLU243
BHOH418

site_idAD1
Number of Residues10
Detailsbinding site for residue 1PG B 303
ChainResidue
ALEU140
AMPD304
BGLY106
BLEU108
BHIS143
BLYS145
BASN175
BTYR205
BARG238
BHOH496

site_idAD2
Number of Residues11
Detailsbinding site for residue 1PG B 304
ChainResidue
AGLU100
AMPD302
BLEU169
BASN173
BSER174
BASN175
BVAL177
BGLU202
BLYS203
BTYR205
BHOH651

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

PDB statisticsPDBj update infoContact PDBjnumon