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3PQB

The crystal structure of pregilvocarcin in complex with GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0071949molecular_functionFAD binding
C0000166molecular_functionnucleotide binding
C0016491molecular_functionoxidoreductase activity
C0050660molecular_functionflavin adenine dinucleotide binding
C0071949molecular_functionFAD binding
D0000166molecular_functionnucleotide binding
D0016491molecular_functionoxidoreductase activity
D0050660molecular_functionflavin adenine dinucleotide binding
D0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 499
ChainResidue
ACYS60
ASER101
AGLY123
AALA124
ACYS125
AVAL128
AGLY129
AGLY131
AGLY132
ALEU133
AGLY138
AARG61
ATYR139
AGLY192
AGLY193
AGLY196
AVAL198
ATYR445
AASN447
AVGP500
AHOH506
AHOH512
ASER62
AHOH521
AHOH539
AHOH596
AGLY63
AGLY64
AHIS65
ACYS66
APHE70
ALEU82

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE VGP A 500
ChainResidue
AHIS65
AGLY67
AALA124
ACYS125
ATYR139
AGLY140
APRO141
APHE265
AGLN328
ASER341
AMET374
AASN376
ASER402
ATYR448
AFAD499
AHOH527
AHOH590

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD B 499
ChainResidue
BCYS60
BARG61
BSER62
BGLY63
BGLY64
BHIS65
BCYS66
BPHE70
BLEU82
BSER101
BGLY123
BALA124
BCYS125
BVAL128
BGLY129
BGLY131
BGLY132
BLEU133
BGLY138
BTYR139
BGLY192
BGLY193
BGLY196
BVAL198
BTYR445
BASN447
BVGP500
BHOH506
BHOH525
BHOH569

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE VGP B 500
ChainResidue
BHIS65
BGLY67
BALA124
BCYS125
BTYR139
BGLY140
BPRO141
BPHE265
BPHE269
BGLN328
BSER341
BMET374
BASN376
BSER402
BTYR448
BFAD499
BHOH657

site_idAC5
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD C 499
ChainResidue
CGLY63
CGLY64
CHIS65
CCYS66
CPHE70
CLEU82
CSER101
CGLY123
CALA124
CCYS125
CVAL128
CGLY129
CGLY131
CGLY132
CLEU133
CTYR139
CGLY192
CGLY193
CGLY196
CVAL198
CTYR445
CASN447
CVGP500
CHOH514
CHOH518
CHOH559
CHOH560
CCYS60
CARG61
CSER62

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE VGP C 500
ChainResidue
CHIS65
CGLY67
CALA124
CCYS125
CTYR139
CGLY140
CPRO141
CPHE265
CMET281
CGLN328
CSER341
CMET374
CASN376
CSER402
CPHE404
CTYR448
CFAD499
CHOH531
CHOH535
CHOH538
CHOH555

site_idAC7
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD D 499
ChainResidue
DCYS60
DARG61
DSER62
DGLY63
DGLY64
DHIS65
DCYS66
DPHE70
DLEU82
DSER101
DGLY123
DALA124
DCYS125
DVAL128
DGLY129
DGLY131
DGLY132
DLEU133
DGLY138
DTYR139
DGLY192
DGLY193
DGLY196
DVAL198
DTYR445
DASN447
DVGP500
DHOH573
DHOH580

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE VGP D 500
ChainResidue
DHIS65
DALA124
DCYS125
DTYR139
DGLY140
DPRO141
DPHE265
DPHE269
DMET281
DGLN328
DVAL334
DSER341
DMET374
DASN376
DSER402
DTYR448
DFAD499
DHOH529
DHOH596

Functional Information from PROSITE/UniProt
site_idPS00862
Number of Residues34
DetailsOX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PeefflpaTpdDVvasLqkavtegrg...VacrSGGH
ChainResidueDetails
APRO32-HIS65

221051

PDB entries from 2024-06-12

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