Structure of PDB 2ve4 Chain A

Receptor sequence

>2ve4A (length=431) Species: 1148 (Synechocystis sp. PCC 6803)

LPIPPGDFGLPWLGETLNFLNDGDFGKKRQQQFGPIFKTRLFGKNVIFIS
GALANRFLFTKEQETFQATWPLSTRILLGPNALATQMGEIHRSRRKILYQ
AFLPRTLDSYLPKMDGIVQGYLEQWGKANEVIWYPQLRRMTFDVAATLFM
GEKVSQNPQLFPWFETYIQGLFSLPIPLPNTLFGKSQRARALLLAELEKI
IKARQQQPPSEEDALGILLAARDDNNQPLSLPELKDQILLLLFAGHETLT
SALSSFCLLLGQHSDIRERVRQEQNKLQLSQELTAETLKKMPYLDQVLQE
VLRLIPPVGGGFRELIQDCQFQGFHFPKGWLVSYQISQTHADPDLYPDPE
KFDPERFTPDGSATHNPPFAHVPFGGGLRECLGKEFARLEMKLFATRLIQ
QFDWTLLPGQNLELVVTPSPRPKDNLRVKLH

3D structure

• PDB: 2ve4 Crystal Structures of Substrate-Free and Retinoic Acid-Bound Cyanobacterial Cytochrome P450 Cyp120A1.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A254 E257 T258 L259 F384 C391 E400
• Catalytic site (residue number reindexed from 1): A244 E247 T248 L249 F374 C381 E390
• Enzyme Commision number: 1.14.-.-

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	HEM	A	L93 H101 R105 A254 G255 T258 L259 P317 V318 R323 Y344 P383 F384 G385 R389 C391 G393 F396 A397	L83 H91 R95 A244 G245 T248 L249 P307 V308 R313 Y334 P373 F374 G375 R379 C381 G383 F386 A387

Gene Ontology

Molecular Function

• GO:0004497 monooxygenase activity
• GO:0005506 iron ion binding
• GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
• GO:0020037 heme binding
• GO:0046872 metal ion binding

Biological Process

• GO:0016125 sterol metabolic process

External links

• PDB: RCSB:2ve4, PDBe:2ve4, PDBj:2ve4
• PDBsum: 2ve4
• PubMed: 18512957
• UniProt: Q59990|CP120_SYNY3 Putative cytochrome P450 120 (Gene Name=cyp120)