Structure of PDB 5mz2 Chain H

Receptor sequence

>5mz2H (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: H
• 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	MG	H	K205 D207 E208	K202 D204 E205
BS02	CAP	H	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
BS03	CAP	H	T69 N127	T66 N124

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