Structure of PDB 3rn1 Chain A

Receptor sequence

>3rn1A (length=354) Species: 318586 (Paracoccus denitrificans PD1222)

ADDALAALGAQLFVDPALSRNATQSCATCHDPARAFTDPREGKAGLAVSV
GDDGQSHGDRNTPTLGYAALVPAFHRDANGKYKGGQFWDGRADDLKQQAG
QPMLNPVEMAMPDRAAVAARLRDDPAYRTGFEALFGKGVLDDPERAFDAA
AEALAAYQATGEFSPFDSKYDRVMRGEEKFTPLEEFGYTVFITENCRLCH
MQRKQGVAERETFTNFEYHNIGLPVNETAREASGLGADHVDHGLLARPGI
EDPAQSGRFKVPSLRNVAVTGPYMHNGVFTDLRTAILFYNKYTSRRPEAK
INPETGAPWGEPEVARNLSLAELQSGLMLDDGRVDALVAFLETLTDRRYE
PLLE

3D structure

• PDB: 3rn1 Mutagenesis of tryptophan199 reveals that electron hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis
• Chain: A
• Resolution: 1.93 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E113
• Catalytic site (residue number reindexed from 1): E108
• Enzyme Commision number: 1.-.-.-

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CA	A	N66 T275 P277	N61 T270 P272
BS02	HEC	A	Q29 C31 C34 H35 R65 T67 P68 L70 Q91 F92 W93 R96 Q103 P107 M114 Q163 K265	Q24 C26 C29 H30 R60 T62 P63 L65 Q86 F87 W88 R91 Q98 P102 M109 Q158 K260
BS03	HEC	A	N200 C201 C204 H205 H224 L228 F264 P267 L269 V272 Y278 M279 H280 Y294	N195 C196 C199 H200 H219 L223 F259 P262 L264 V267 Y273 M274 H275 Y289

Gene Ontology

Molecular Function

• GO:0004130 cytochrome-c peroxidase activity
• GO:0009055 electron transfer activity
• GO:0016491 oxidoreductase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding

Biological Process

• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0042597 periplasmic space

External links

• PDB: RCSB:3rn1, PDBe:3rn1, PDBj:3rn1
• PDBsum: 3rn1
• UniProt: Q51658|MAUG_PARDP Methylamine utilization protein MauG (Gene Name=mauG)