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2B5W

Crystal structure of D38C glucose dehydrogenase mutant from Haloferax mediterranei

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005536molecular_functionD-glucose binding
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0019595biological_processnon-phosphorylated glucose catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0047934molecular_functionglucose 1-dehydrogenase (NAD+) activity
A0047935molecular_functionglucose 1-dehydrogenase (NADP+) activity
A0047936molecular_functionglucose 1-dehydrogenase [NAD(P)+] activity
A0070401molecular_functionNADP+ binding
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 800
ChainResidue
ACYS38
AHIS63
AGLU64
AHOH1543

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FLC A 802
ChainResidue
AHOH945
AHOH1009
AHOH1131
AHOH1144
AHOH1180
AHOH1225
AHOH1266
AHOH1284
AHOH1333
AHOH1470
AHOH1507
ASER228
APHE252
ALYS254
AHIS255
ANAP701

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 901
ChainResidue
AASP344
ATHR347
AHOH929
AHOH988
AHOH1000
AHOH1340

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 902
ChainResidue
AASP172
APRO173
ALYS197
AGLY198
AHOH1129
AHOH1184

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K A 903
ChainResidue
ATHR315
AHOH923
AHOH924
AHOH965
AHOH982
AHOH1025
AHOH1107

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 904
ChainResidue
APRO237
AASP238
ATYR240
AHOH1574

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A 905
ChainResidue
AHOH1048
AHOH1055
AHOH1068

site_idAC8
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NAP A 701
ChainResidue
AGLY39
AGLU43
AASN181
AGLY182
ASER183
ALEU184
AGLY206
AARG207
AARG208
ASER228
AALA249
AGLY251
APHE252
AHIS255
ALEU272
AVAL274
AVAL292
ASER301
AVAL302
AASN303
AFLC802
AHOH935
AHOH942
AHOH1000
AHOH1048
AHOH1051
AHOH1055
AHOH1068
AHOH1077
AHOH1108
AHOH1132
AHOH1174
AHOH1204
AHOH1242
AHOH1310
AHOH1311
AHOH1413

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:16551747, ECO:0000269|PubMed:19131516
ChainResidueDetails
ACYS38
AHIS63
AGLU64
AGLU150
AASN181
AARG207
ASER228
ALEU272
ASER301

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19131516
ChainResidueDetails
ATHR40
AHIS49
AGLU114
AASN303

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
ATHR40
AGLY39

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
AHIS49

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PDB entries from 2025-06-18

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