Structure of PDB 1krh Chain B Binding Site BS02

Receptor Information
>1krh Chain B (length=337) Species: 472 (Acinetobacter sp.) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SNHQVALQFEDGVTRFICIAQGETLSDAAYRQQINIPMDCREGECGTCRA
FCESGNYDMPEDNYIEDALTPEEAQQGYVLACQCRPTSDAVFQIQASSEV
CKTKIHHFEGTLARVENLSDSTITFDIQLDDGQPDIHFLAGQYVNVTLPG
TTETRSYSFSSQPGNRLTGFVVRNVPQGKMSEYLSVQAKAGDKMSFTGPF
GSFYLRDVKRPVLMLAGGTGIAPFLSMLQVLEQKGSEHPVRLVFGVTQDC
DLVALEQLDALQQKLPWFEYRTVVAHAESQHERKGYVTGHIEYDWLNGGE
VDVYLCGPVPMVEAVRSWLDTQGIQPANFLFEKFSAN
Ligand information
Ligand IDFAD
InChIInChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
InChIKeyVWWQXMAJTJZDQX-UYBVJOGSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P@](O)(=O)O[P@@](O)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)n5cnc6c(N)ncnc56)c2cc1C
OpenEye OEToolkits 1.5.0Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)n5cnc6c5ncnc6N)O)O)O)O)O
OpenEye OEToolkits 1.5.0Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](CO[P@@](=O)(O)O[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)n5cnc6c5ncnc6N)O)O)O)O)O
CACTVS 3.341Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH]([CH](O)[CH]4O)n5cnc6c(N)ncnc56)c2cc1C
ACDLabs 10.04O=C2C3=Nc1cc(c(cc1N(C3=NC(=O)N2)CC(O)C(O)C(O)COP(=O)(O)OP(=O)(O)OCC6OC(n5cnc4c(ncnc45)N)C(O)C6O)C)C
FormulaC27 H33 N9 O15 P2
NameFLAVIN-ADENINE DINUCLEOTIDE
ChEMBLCHEMBL1232653
DrugBankDB03147
ZINCZINC000008215434
PDB chain1krh Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1krh X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		Y144 R156 S157 Y158 S159 V173 G179 K180 M181 S182 T220 E333 K334 F335 S336 A337 N338
Binding residue
(residue number reindexed from 1)		Y143 R155 S156 Y157 S158 V172 G178 K179 M180 S181 T219 E332 K333 F334 S335 A336 N337
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) C307
Catalytic site (residue number reindexed from 1) C306
Enzyme Commision number 1.18.1.3: ferredoxin--NAD(+) reductase.
Gene Ontology
Molecular Function
GO:0008860 ferredoxin-NAD+ reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009056 catabolic process
GO:0042203 toluene catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1krh, PDBe:1krh, PDBj:1krh
PDBsum1krh
PubMed12051836
UniProtP07771|BENC_ACIAD Benzoate 1,2-dioxygenase electron transfer component (Gene Name=benC)

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