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6D0P

1.88 Angstrom Resolution Crystal Structure of Quercetin 2,3-dioxygenase from Acinetobacter baumannii

Functional Information from GO Data
ChainGOidnamespacecontents
A0008127molecular_functionquercetin 2,3-dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0008127molecular_functionquercetin 2,3-dioxygenase activity
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
C0008127molecular_functionquercetin 2,3-dioxygenase activity
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
D0008127molecular_functionquercetin 2,3-dioxygenase activity
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 301
ChainResidue
AHOH416
AHOH519
AHOH525
AHOH605
AHOH651
AHOH690

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 302
ChainResidue
AHOH622
AHOH717
BHOH458
ALEU153
AHOH510
AHOH618

site_idAC3
Number of Residues6
Detailsbinding site for residue MN A 303
ChainResidue
AHIS61
AHIS63
AHIS105
AGLU107
AHOH405
AHOH563

site_idAC4
Number of Residues10
Detailsbinding site for residue PEG A 304
ChainResidue
AVAL16
AASP42
AVAL58
AHIS61
AGLU107
AMSE122
AGLN124
AHOH405
AHOH410
AHOH465

site_idAC5
Number of Residues4
Detailsbinding site for residue PEG A 305
ChainResidue
ATYR260
AHOH450
AHOH554
BHIS14

site_idAC6
Number of Residues5
Detailsbinding site for residue PG4 A 306
ChainResidue
ATYR260
AGLY261
AHOH572
BPRO262
BPHE278

site_idAC7
Number of Residues3
Detailsbinding site for residue CL B 301
ChainResidue
AALA152
AHOH674
BASN48

site_idAC8
Number of Residues6
Detailsbinding site for residue MN B 302
ChainResidue
BHIS61
BHIS63
BHIS105
BGLU107
BHOH533
BHOH537

site_idAC9
Number of Residues6
Detailsbinding site for residue PEG B 303
ChainResidue
BASP42
BMSE122
BGLN124
BTRP126
BEDO304
BHOH576

site_idAD1
Number of Residues2
Detailsbinding site for residue EDO B 304
ChainResidue
BVAL58
BPEG303

site_idAD2
Number of Residues4
Detailsbinding site for residue PG4 B 305
ChainResidue
AHIS14
ATYR28
BTYR260
BHOH474

site_idAD3
Number of Residues6
Detailsbinding site for residue MN C 301
ChainResidue
CHIS61
CHIS63
CHIS105
CGLU107
CHOH402
CHOH499

site_idAD4
Number of Residues8
Detailsbinding site for residue PEG C 302
ChainResidue
CVAL16
CASP42
CVAL58
CGLU107
CMSE122
CHOH402
CHOH423
CHOH445

site_idAD5
Number of Residues3
Detailsbinding site for residue GOL C 303
ChainResidue
CTRP15
CGLY17
CASP18

site_idAD6
Number of Residues4
Detailsbinding site for residue CL D 301
ChainResidue
DLEU5
DSER229
DARG230
DHOH602

site_idAD7
Number of Residues6
Detailsbinding site for residue MN D 302
ChainResidue
DHIS61
DHIS63
DHIS105
DGLU107
DHOH405
DHOH537

site_idAD8
Number of Residues9
Detailsbinding site for residue PGE D 303
ChainResidue
DVAL16
DASP42
DVAL58
DHIS61
DGLU107
DMSE122
DHOH405
DHOH423
DHOH488

site_idAD9
Number of Residues9
Detailsbinding site for residue PG4 D 304
ChainResidue
DASP184
DGLY185
DLYS244
DHOH406
DTYR73
DGLY92
DGLU121
DHIS159
DARG161

218853

PDB entries from 2024-04-24

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