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1KV9

Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5

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
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0070968molecular_functionpyrroloquinoline quinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 802
ChainResidue
AGLU173
AASN250
AASP295
APQQ801

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE PQQ A 801
ChainResidue
ATHR155
AGLY170
AGLY171
AALA172
AGLU173
ATHR230
ATRP232
AASN250
AASP295
ALYS322
AASN382
ATRP383
ATRP460
AGLY524
AVAL525
ACA802
AACN803
AHOH1114
AHOH1210
AGLU59
ACYS105
ACYS106
AVAL109
AARG111

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC A 901
ChainResidue
AALA101
AARG102
APHE590
ACYS591
ACYS594
AHIS595
AILE605
APRO606
ALEU608
ASER611
APHE619
AVAL623
ALEU631
AMET633
APHE636
ALEU640
AHOH1091
AHOH1139
AHOH1242
AHOH1362
AHOH1514

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE EPE A 804
ChainResidue
ATRP48
AALA83
AALA84
ASER85
ATYR515
AHOH1178
AHOH1528
AHOH1614
AHOH1683
AHOH1687
AHOH1735

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACN A 803
ChainResidue
AGLU173
AASP295
ALYS322
APRO377
APQQ801

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 805
ChainResidue
AASP51
ALEU52
ASER543
AHOH1392
AHOH1531

Functional Information from PROSITE/UniProt
site_idPS00364
Number of Residues22
DetailsBACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WdsmaYDpelDLLYVgtGngSP
ChainResidueDetails
ATRP232-PRO253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues78
DetailsDomain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12057198","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12057198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KV9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"12057198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KV9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12057198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KV9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
AASP295

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PDB entries from 2025-12-17

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