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1YIQ

Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase ADHIIG from Pseudomonas putida HK5. Compariison to the other quinohemoprotein alcohol dehydrogenase ADHIIB found in the same microorganism.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050039molecular_functionlactaldehyde reductase (NADPH) activity
A0070968molecular_functionpyrroloquinoline quinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 802
ChainResidue
AGLU178
AASN255
AASP300
APQQ801
APGR803

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE PQQ A 801
ChainResidue
AARG115
ATHR160
AGLY175
AGLY176
AALA177
AGLU178
ATHR235
ATRP237
AASN255
AASP300
ALYS327
ATRP386
AASP390
ATRP391
APHE477
AALA542
ACA802
APGR803
AHOH1079
AHOH1108
AGLU63
ACYS109
ACYS110
AVAL113

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEC A 901
ChainResidue
AARG60
AGLY106
ATYR605
ACYS606
AGLN608
ACYS609
AHIS610
ALEU623
ALEU626
ALYS630
ALEU638
AARG642
AASP645
AGLY646
AMET647
APHE650
APHE654
AHOH1088
AHOH1303
AHOH1373

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGR A 803
ChainResidue
ACYS110
AGLU178
AASP300
ATRP386
AALA542
APQQ801
ACA802
AHOH1271

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGR A 804
ChainResidue
AGLU441
AILE595
ATYR665
ALYS668

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGR A 805
ChainResidue
ALEU552
AARG579
ASER616
AASP622
AARG624
ALYS625
AHOH1201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:16061256
ChainResidueDetails
AASP300

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q46444
ChainResidueDetails
AGLU63
AALA542

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:16061256, ECO:0007744|PDB:1YIQ
ChainResidueDetails
AARG115
AASP390
ATHR160
AGLY176
AGLU178
ATHR235
AASN255
AASP300
ALYS327
ATRP386

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:16061256, ECO:0007744|PDB:1YIQ
ChainResidueDetails
ACYS606
ACYS609

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:16061256, ECO:0007744|PDB:1YIQ
ChainResidueDetails
AHIS610
AMET647

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
AASP300

226707

PDB entries from 2024-10-30

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