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2B5V

Crystal structure of glucose dehydrogenase 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 Residues25
DetailsBINDING SITE FOR RESIDUE NAP A 501
ChainResidue
AASP38
ASER228
AALA249
AGLY251
AHIS255
ALEU272
AVAL274
AVAL292
ASER301
AVAL302
AASN303
AGLY180
AHOH503
AHOH505
AHOH543
AHOH548
AHOH559
AHOH614
AASN181
AGLY182
ASER183
ALEU184
AGLY206
AARG207
AARG208

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

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PDB entries from 2024-11-06

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