Structure of PDB 4c9l Chain B

Receptor sequence
>4c9lB (length=407) Species: 48935 (Novosphingobium aromaticivorans) [Search protein sequence]
KHRVAPPPHVPGHLIREIDAYDLDGLEQGFHEAWKRVQQPDTPPLVWTPF
TGGHWIATRGTLIDEIYRSPERFSSRVIWVPREAGEAYDMVPTKLDPPEH
TPYRKAIDKGLNLAEIRKLEDQIRTIAVEIIEGFADRGHCEFGSEFSTVF
PVRVFLALAGLPVEDATKLGLLANEMTRPSGNTPEEQGRSLEAANKGFFE
YVAPIIAARRGGSGTDLITRILNVEIDGKPMPDDRALGLVSLLLLGGLDT
VVNFLGFMMIYLSRHPETVAEMRREPLKLQRGVEELFRRFAVVSDARYVV
SDMEFHGTMLKEGDLILLPTALHGLDDRHHDDPMTVDLSRRDVTHSTFAQ
GPHRCAGMHLARLEVTVMLQEWLARIPEFRLKDRAVPIYHSGIVAAVENI
PLEWEPQ
3D structure
PDB4c9l Crystal Structures and Functional Characterization of Wild Type and Active Sites Mutants of Cyp101D1.
ChainB
Resolution1.801 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R188 G256 D259 T260 V261 C365 A366 G367 E374 V404
Catalytic site (residue number reindexed from 1) R178 G246 D249 T250 V251 C355 A356 G357 E364 V394
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 B P102 T103 H110 R114 G256 T260 V261 V303 D305 R307 T357 F358 A359 H363 C365 G367 P92 T93 H100 R104 G246 T250 V251 V293 D295 R297 T347 F348 A349 H353 C355 G357
BS02 CAM B W89 Y98 W79 Y88
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:4c9l, PDBe:4c9l, PDBj:4c9l
PDBsum4c9l
PubMed24261604
UniProtQ2GB12

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