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1EZ0

CRYSTAL STRUCTURE OF THE NADP+ DEPENDENT ALDEHYDE DEHYDROGENASE FROM VIBRIO HARVEYI.

Replaces:  1CO3
Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0033721molecular_functionaldehyde dehydrogenase (NADP+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAP A 650
ChainResidue
ASER146
AASN147
ALYS172
AHIS174
ATHR175
AARG210
AGLN214
APHE227
ATHR228
AGLY229
ASER230
AGLY233
AGLU253
ACYS289
AGLU377
APHE379
ALEU405
AHIS450
AHOH1028
AHOH1118

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAP B 750
ChainResidue
AASP6
BPHE143
BSER146
BASN147
BLYS172
BHIS174
BTHR175
BARG210
BGLN214
BPHE227
BTHR228
BGLY229
BSER230
BGLY233
BLEU237
BGLU253
BCYS289
BGLU377
BPHE379
BLEU405
BHIS450
BHOH1282
BHOH1313

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP C 850
ChainResidue
CSER146
CASN147
CLYS172
CHIS174
CTHR175
CARG210
CGLN214
CPHE227
CTHR228
CGLY229
CSER230
CGLY233
CLEU237
CGLU253
CCYS289
CGLU377
CPHE379
CLEU405
CHIS450
CHOH1353
CHOH1442

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP D 950
ChainResidue
DGLY233
DLEU237
DGLU253
DGLY255
DCYS289
DGLU377
DPHE379
DLEU405
DHOH1517
DHOH1607
DSER146
DASN147
DLYS172
DHIS174
DTHR175
DARG210
DGLN214
DPHE227
DTHR228
DGLY229
DSER230

site_idCTA
Number of Residues2
DetailsTHE KEY RESIDUES AROUND THE ACTIVE SITE
ChainResidue
AGLU253
ACYS289

site_idCTB
Number of Residues2
DetailsTHE KEY RESIDUES AROUND THE ACTIVE SITE
ChainResidue
BGLU253
BCYS289

site_idCTC
Number of Residues2
DetailsTHE KEY RESIDUES AROUND THE ACTIVE SITE
ChainResidue
CGLU253
CCYS289

site_idCTD
Number of Residues2
DetailsTHE KEY RESIDUES AROUND THE ACTIVE SITE
ChainResidue
DGLU253
DCYS289

site_idNPA
Number of Residues4
DetailsKEY RESIDUES WHICH INTERACT WITH THE NADP+ COFACTOR
ChainResidue
ALYS172
ATHR175
AARG210
AGLU377

site_idNPB
Number of Residues4
DetailsKEY RESIDUES WHICH INTERACT WITH THE NADP+ COFACTOR
ChainResidue
BTHR175
BARG210
BGLU377
BLYS172

site_idNPC
Number of Residues4
DetailsKEY RESIDUES WHICH INTERACT WITH THE NADP+ COFACTOR
ChainResidue
CLYS172
CTHR175
CARG210
CGLU377

site_idNPD
Number of Residues4
DetailsKEY RESIDUES WHICH INTERACT WITH THE NADP+ COFACTOR
ChainResidue
DLYS172
DTHR175
DARG210
DGLU377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE:
ChainResidueDetails
CGLU253
CCYS289
DGLU253
DCYS289
AGLU253
ACYS289
BGLU253
BCYS289

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLY229
BGLY229
CGLY229
DGLY229

218500

PDB entries from 2024-04-17

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