Structure of PDB 3rup Chain B

Receptor sequence

>3rupB (length=446) Species: 83333 (Escherichia coli K-12) [Search protein sequence]

MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVC
IGPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGF
IFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRAIAK
RIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDMVYM
EKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPGITP
ELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVT
EMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPS
PGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIA
RMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKLGL

3D structure

PDB

3rup Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization.

Chain

Resolution

1.99 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	K116 K159 D196 H209 R235 T274 E276 E288 N290 R292 E296 R338
Catalytic site (residue number reindexed from 1)	K116 K159 D196 H209 R235 T274 E276 E288 N290 R292 E296 R338
Enzyme Commision number	6.3.4.14: biotin carboxylase.

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	ADP	B	K116 K159 G164 G166 M169 E201 K202 Y203 L204 H209 Q233 H236 L278 E288 I437	K116 K159 G164 G166 M169 E201 K202 Y203 L204 H209 Q233 H236 L278 E288 I437
BS02	ADP	B	G83 G164 G165 K238 R292 Q294 V295 E296 R338 D382	G83 G164 G165 K238 R292 Q294 V295 E296 R338 D382
BS03	CA	B	E276 E288	E276 E288
BS04	CA	B	E87 E288 N290	E87 E288 N290

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0003989	acetyl-CoA carboxylase activity
GO:0004075	biotin carboxylase activity
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0016874	ligase activity
GO:0042803	protein homodimerization activity
GO:0046872	metal ion binding

	Biological Process
GO:0006633	fatty acid biosynthetic process
GO:0045717	negative regulation of fatty acid biosynthetic process
GO:2001295	malonyl-CoA biosynthetic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0009317	acetyl-CoA carboxylase complex

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:3rup, PDBe:3rup, PDBj:3rup
PDBsum	3rup
PubMed	21592965
UniProt	P24182\|ACCC_ECOLI Biotin carboxylase (Gene Name=accC)

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