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2VWQ

Haloferax mediterranei glucose dehydrogenase in complex with NADP and Zn.

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 Residues21
DetailsBINDING SITE FOR RESIDUE NAP A 500
ChainResidue
AILE154
AALA249
AGLY251
AHIS255
ALEU272
AVAL274
AVAL292
ASER301
AVAL302
AASN303
AHOH2057
AASN181
AHOH2110
AHOH2112
AGLY182
ASER183
ALEU184
AGLY206
AARG207
AARG208
ASER228

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 800
ChainResidue
AASP38
AHIS63
AGLU64
AGLU150
AHOH2113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:16551747, ECO:0000269|PubMed:19131516
ChainResidueDetails
AASP38
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 2024-07-24

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