Structure of PDB 4c9n Chain A

Receptor sequence
>4c9nA (length=408) Species: 48935 (Novosphingobium aromaticivorans) [Search protein sequence]
QKHRVAPPPHVPGHLIREIDAYDLDGLEQGFHEAWKRVQQPDTPPLVWTP
FTGGHWIATRGTLIDEIYRSPERFSSRVIWVPREAGEAYDMVPTKLDPPE
HTPYRKAIDKGLNLAEIRKLEDQIRTIAVEIIEGFADRGHCEFGSEFSTV
FPVRVFLALAGLPVEDATKLGLLANEMTRPSGNTPEEQGRSLEAANKGFF
EYVAPIIAARRGGSGTDLITRILNVEIDGKPMPDDRALGLVSLLLLGGLN
TVVNFLGFMMIYLSRHPETVAEMRREPLKLQRGVEELFRRFAVVSDARYV
VSDMEFHGTMLKEGDLILLPTALHGLDDRHHDDPMTVDLSRRDVTHSTFA
QGPHRCAGMHLARLEVTVMLQEWLARIPEFRLKDRAVPIYHSGIVAAVEN
IPLEWEPQ
3D structure
PDB4c9n Crystal Structures and Functional Characterization of Wild Type and Active Sites Mutants of Cyp101D1.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R188 G256 N259 T260 V261 C365 A366 G367 E374 V404
Catalytic site (residue number reindexed from 1) R179 G247 N250 T251 V252 C356 A357 G358 E365 V395
Enzyme Commision number ?
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 P102 H110 R114 F165 L252 G256 T260 V303 D305 R307 T357 F358 A359 H363 C365 A366 G367 P93 H101 R105 F156 L243 G247 T251 V294 D296 R298 T348 F349 A350 H354 C356 A357 G358
BS02 CAM A W89 Y98 L255 W80 Y89 L246
BS03 CAH A W89 Y98 L252 L255 W80 Y89 L243 L246
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
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:4c9n, PDBe:4c9n, PDBj:4c9n
PDBsum4c9n
PubMed24261604
UniProtQ2GB12

[Back to BioLiP]