Structure of PDB 3oma Chain A

Receptor sequence

>3omaA (length=535) Species: 272943 (Cereibacter sphaeroides 2.4.1) [Search protein sequence]

FTRWFMSTNHKDIGVLYLFTGGLVGLISVAFTVYMRMELMAPGVQFMCAE
HLESGLVKGFFQSLWPSAVENCTPNGHLWNVMITGHGILMMFFVVIPALF
GGFGNYFMPLHIGAPDMAFPRMNNLSYWLYVAGTSLAVASLFAPGGNGQL
GSGIGWVLYPPLSTSESGYSTDLAIFAVHLSGASSILGAINMITTFLNMR
APGMTMHKVPLFAWSIFVTAWLILLALPVLAGAITMLLTDRNFGTTFFQP
SGGGDPVLYQHILWFFGHPEVYIIVLPAFGIVSHVIATFAKKPIFGYLPM
VYAMVAIGVLGFVVWAHHMYTAGLSLTQQSYFMMATMVIAVPTGIMIFSW
IATMWGGSIELKTPMLWALGFLFLFTVGGVTGIVLSQASVDRYYHDTYYV
VAHFHYVMSLGAVFGIFAGIYFWIGKMSGRQYPEWAGKLHFWMMFVGANL
TFFPQHFLGRQGMPRRYIDYPEAFATWNFVSSLGAFLSFASFLFFLGVIF
YTLTRGARVTANNYWNEHADTLEWTLTSPPPEHTF

3D structure

PDB

3oma Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump.

Chain

Resolution

2.3 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y33 I43 F47 M51 I99 H102 N121 D132 N139 S142 Y146 W172 S200 S201 G204 T211 H284 E286 Y288 S299 P315 H333 H334 T359 M362 H419 F420 H421 R481
Catalytic site (residue number reindexed from 1)	Y17 I27 F31 M35 I83 H86 N105 D116 N123 S126 Y130 W156 S184 S185 G188 T195 H268 E270 Y272 S283 P299 H317 H318 T343 M346 H403 F404 H405 R465
Enzyme Commision number	7.1.1.9: cytochrome-c oxidase.

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)
BS01	DMU	A	M56 Q61 F502	M40 Q45 F486
BS02	HEA	A	G38 T48 M51 R52 W95 I99 H102 M106 M107 G171 W172 Y414 F420 H421 M424 S425 V429 M460 F468 R481 R482 S504	G22 T32 M35 R36 W79 I83 H86 M90 M91 G155 W156 Y398 F404 H405 M408 S409 V413 M444 F452 R465 R466 S488
BS03	HEA	A	W172 W280 V287 Y288 H333 H334 G360 G395 G398 I399 L401 S402 D407 H411 H419 F420 V423 M424 R481	W156 W264 V271 Y272 H317 H318 G344 G379 G382 I383 L385 S386 D391 H395 H403 F404 V407 M408 R465
BS04	CU	A	H284 H333 H334	H268 H317 H318
BS05	MG	A	H411 D412	H395 D396
BS06	CA	A	E54 A57 G59 Q61	E38 A41 G43 Q45

Gene Ontology

	Molecular Function
GO:0004129	cytochrome-c oxidase activity
GO:0016491	oxidoreductase activity
GO:0020037	heme binding
GO:0046872	metal ion binding

	Biological Process
GO:0006119	oxidative phosphorylation
GO:0009060	aerobic respiration
GO:0015990	electron transport coupled proton transport
GO:0022904	respiratory electron transport chain

	Cellular Component
GO:0005886	plasma membrane
GO:0016020	membrane
GO:0045277	respiratory chain complex IV

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:3oma, PDBe:3oma, PDBj:3oma
PDBsum	3oma
PubMed	21205904
UniProt	Q3J5A7

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