Structure of PDB 3orv Chain A

Receptor sequence

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

ADDALAALGAQLFVDPALSRNATQSCATCHDPARAFTDPREGKAGLAVSV
GDDGQSHGDRNTPTLGYAALVPAFHRDANGKYKGGQFWDGRADDLKQQAG
QPMLNPVEMAMPDRAAVAARLRDDPAYRTGFEALFGKGVLDDPERAFDAA
AEALAAYQATGEFSPFDSKYDRVMRGEEKFTPLEEFGYTVFITWNCRLCH
MQRKQGVAERETFTNFEYHNIGLPVNETAREASGLGADHVDHGLLARPGI
EDPAQSGRFKVPSLRNVAVTGPYMHNGVFTDLRTAILFHNKYTSRRPEAK
INPETGAPWGEPEVARNLSLAELQSGLMLDDGRVDALVAFLETLTDRRYE
PLLE

3D structure

• PDB: 3orv Functional Importance of Tyrosine 294 and the Catalytic Selectivity for the Bis-Fe(IV) State of MauG Revealed by Replacement of This Axial Heme Ligand with Histidine .
• Chain: A
• Resolution: 1.91 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 K265	Q24 C26 C29 H30 R60 T62 P63 L65 Q86 F87 W88 R91 Q98 P102 M109 K260
BS03	HEC	A	N200 C201 C204 H205 H224 I226 L228 F264 P267 L269 Y278 M279 H280 H294	N195 C196 C199 H200 H219 I221 L223 F259 P262 L264 Y273 M274 H275 H289

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:3orv, PDBe:3orv, PDBj:3orv
• PDBsum: 3orv
• PubMed: 20929212
• UniProt: Q51658|MAUG_PARDP Methylamine utilization protein MauG (Gene Name=mauG)