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1KB0

Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 801
ChainResidue
AGLU185
AASN263
AASP308
APQQ1800
ATFB1810

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEC A 802
ChainResidue
ACYS607
AHIS608
APRO620
AMET625
ATYR629
ALEU633
APHE636
APRO641
AALA642
AARG645
AGLY646
AMET647
APRO648
APHE650
AHOH2067
AHOH2541
AHOH2726
AARG67
AGLN435
AASN603
ACYS604

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TFB A 1810
ChainResidue
ACYS116
ACYS117
AGLU185
ATRP267
AASP308
APRO389
ATRP440
ACA801
APQQ1800
AHOH2840

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE PQQ A 1800
ChainResidue
AGLU70
ACYS116
ACYS117
AVAL120
AARG122
ATHR167
AGLY182
AGLY183
AALA184
AGLU185
ATHR243
ATRP245
AASN263
AASP308
ALYS335
AASN394
ATRP395
ATRP479
AGLY543
AVAL544
ACA801
ATFB1810
AHOH1845
AHOH1856

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1820
ChainResidue
AGLU474
AHIS475
AARG499
ATYR503
ALYS510
AHOH1866
AHOH2611

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1823
ChainResidue
ATRP541
AARG550
ATHR552
AARG554
AGLN555
AGLY617
AASN618
AHOH1913
AHOH1945
AHOH2575

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1824
ChainResidue
AHOH2447
AHOH2635

Functional Information from PROSITE/UniProt
site_idPS00364
Number of Residues22
DetailsBACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WdsmtFDaelNTMYVgtGngSP
ChainResidueDetails
ATRP245-PRO266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:11714714
ChainResidueDetails
AASP308

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:11714714, ECO:0007744|PDB:1KB0
ChainResidueDetails
AGLU70
AASN394
AVAL544
AARG122
ATHR167
AGLY183
AGLU185
ATHR243
AASN263
AASP308
ALYS335

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:11714714, ECO:0007744|PDB:1KB0
ChainResidueDetails
ACYS604
ACYS607

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11714714, ECO:0007744|PDB:1KB0
ChainResidueDetails
AHIS608
AMET647

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
AASP308

221371

PDB entries from 2024-06-19

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