Structure of PDB 5mz2 Chain E

Receptor sequence

>5mz2E (length=481) Species: 555753 (Thalassiosira antarctica var. borealis)

SVSERTRIKSDRYESGVIPYAKMGYWDAAYSVKDTDILALFRITPQPGVD
PVEAAAAVAGESSTATWTVVWTDLLTACERYRAKAYRVDPVPNSTDVYFA
FIAYECDLFEEASLSNLTASIIGNVFGFKAISALRLEDMRIPHSYLKTFQ
GPATGIIVERERLNKYGTPLLGATVKPKLGLSGKNYGRVVYEGLKGGLDF
LKDDENINSQPFMRWRERFLNCLEGINRAAAATGEVKGSYLNITAATMEE
VYKRAEYAKAIGSVVVMIDLVMGYTAIQSIAYWARENDMLLHLHRAGNST
YARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDILR
LTELEVNLPFGIFFEMDWASLRRCMPVASGGIHCGQMHQLIHYLGDDVVL
QFGGGTIGHPDGIQAGATANRVALEAMVLARNEGADYFNNQVGPQILRDA
AKTCGPLQTALDLWKDISFNYTSTDTADFAE

3D structure

• PDB: 5mz2 Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications.
• Chain: E
• Resolution: 1.9 Å

Enzymatic activity

• Enzyme Commision number: 4.1.1.39: ribulose-bisphosphate 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	CAP	E	T69 N127	T66 N124
BS02	MG	E	K205 D207 E208	K202 D204 E205
BS03	CAP	E	T177 K179 K205 D207 E208 H297 R298 H330 K337 L338 S382 G383 G406 G407	T174 K176 K202 D204 E205 H294 R295 H327 K334 L335 S379 G380 G403 G404

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004497 monooxygenase activity
• GO:0016829 lyase activity
• GO:0016984 ribulose-bisphosphate carboxylase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0015977 carbon fixation
• GO:0015979 photosynthesis
• GO:0019253 reductive pentose-phosphate cycle

Cellular Component

• GO:0009507 chloroplast

External links

• PDB: RCSB:5mz2, PDBe:5mz2, PDBj:5mz2
• PDBsum: 5mz2
• PubMed: 29925588
• UniProt: A8DP67