Structure of PDB 4rzq Chain A

Receptor sequence
>4rzqA (length=422) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence]
HMLEKVVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETI
CIGPAPSAKSYLNIPAIIAAAEVTGADAIHPGYGFLSENADFAEQVERSG
FTFIGPTADVIRLMGDKVSAIKAMKKAGVPCVPGSDGPAKNKEIAKRIGY
PIIIKRVVRSEDALEESIAMTKAEYMEKYLENPRHVEIQVLADTHGNAVY
LAERDCSMQRRHQKVVEEAPAPGITEEVRRDIGSRCANACVEIGYRGAGT
FEFLYENGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQLRIAAGLPISFK
QEDIKVKGHAMECRINAEDPKTFLPSPGKVNHLHSPGGLGVRWDSHVYGG
YTVPPHYDSMIAKLITYGDTREVAIRRMQNALSETIIDGIKTNIPLHELI
LEDENFQKGGTNIHYLEKKLGM
3D structure
PDB4rzq Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.
ChainA
Resolution1.98 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 H209 R235 T274 E276 E288 N290 R292 E296 R338
Catalytic site (residue number reindexed from 1) K117 K155 H185 R211 T250 E252 E264 N266 R268 E272 R314
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)		 Binding affinity
BS01 Y7Y A N9 R10 Y82 F84 K238 R292 Q294 V295 E296 R338 D382 N10 R11 Y83 F85 K214 R268 Q270 V271 E272 R314 D358
BS02 ADP A Y203 L204 L278 Y179 L180 L254
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003989 acetyl-CoA carboxylase activity
GO:0004075 biotin carboxylase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4rzq, PDBe:4rzq, PDBj:4rzq
PDBsum4rzq
PubMed26020841
UniProtP43873|ACCC_HAEIN Biotin carboxylase (Gene Name=accC)

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