Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5IU0

Rubisco from Arabidopsis thaliana

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003729	molecular_function	mRNA binding
A	0004497	molecular_function	monooxygenase activity
A	0005515	molecular_function	protein binding
A	0009505	cellular_component	plant-type cell wall
A	0009507	cellular_component	chloroplast
A	0009535	cellular_component	chloroplast thylakoid membrane
A	0009536	cellular_component	plastid
A	0009570	cellular_component	chloroplast stroma
A	0009579	cellular_component	thylakoid
A	0009737	biological_process	response to abscisic acid
A	0009853	biological_process	photorespiration
A	0009941	cellular_component	chloroplast envelope
A	0015977	biological_process	carbon fixation
A	0015979	biological_process	photosynthesis
A	0016491	molecular_function	oxidoreductase activity
A	0016829	molecular_function	lyase activity
A	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
A	0019253	biological_process	reductive pentose-phosphate cycle
A	0022626	cellular_component	cytosolic ribosome
A	0046686	biological_process	response to cadmium ion
A	0046872	molecular_function	metal ion binding
A	0048046	cellular_component	apoplast
B	0000287	molecular_function	magnesium ion binding
B	0003729	molecular_function	mRNA binding
B	0004497	molecular_function	monooxygenase activity
B	0005515	molecular_function	protein binding
B	0009505	cellular_component	plant-type cell wall
B	0009507	cellular_component	chloroplast
B	0009535	cellular_component	chloroplast thylakoid membrane
B	0009536	cellular_component	plastid
B	0009570	cellular_component	chloroplast stroma
B	0009579	cellular_component	thylakoid
B	0009737	biological_process	response to abscisic acid
B	0009853	biological_process	photorespiration
B	0009941	cellular_component	chloroplast envelope
B	0015977	biological_process	carbon fixation
B	0015979	biological_process	photosynthesis
B	0016491	molecular_function	oxidoreductase activity
B	0016829	molecular_function	lyase activity
B	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
B	0019253	biological_process	reductive pentose-phosphate cycle
B	0022626	cellular_component	cytosolic ribosome
B	0046686	biological_process	response to cadmium ion
B	0046872	molecular_function	metal ion binding
B	0048046	cellular_component	apoplast
I	0003729	molecular_function	mRNA binding
I	0009507	cellular_component	chloroplast
I	0009536	cellular_component	plastid
I	0009570	cellular_component	chloroplast stroma
I	0009579	cellular_component	thylakoid
I	0009853	biological_process	photorespiration
I	0009941	cellular_component	chloroplast envelope
I	0015977	biological_process	carbon fixation
I	0015979	biological_process	photosynthesis
I	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
I	0019253	biological_process	reductive pentose-phosphate cycle
I	0019904	molecular_function	protein domain specific binding
I	0048046	cellular_component	apoplast
J	0003729	molecular_function	mRNA binding
J	0009507	cellular_component	chloroplast
J	0009536	cellular_component	plastid
J	0009570	cellular_component	chloroplast stroma
J	0009579	cellular_component	thylakoid
J	0009853	biological_process	photorespiration
J	0009941	cellular_component	chloroplast envelope
J	0015977	biological_process	carbon fixation
J	0015979	biological_process	photosynthesis
J	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
J	0019253	biological_process	reductive pentose-phosphate cycle
J	0019904	molecular_function	protein domain specific binding
J	0048046	cellular_component	apoplast

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue MG A 501

Chain	Residue
A	KCX201
A	ASP203
A	GLU204
A	CAP502

site_id	AC2
Number of Residues	26
Details	binding site for residue CAP A 502

Chain	Residue
A	GLU204
A	HIS294
A	ARG295
A	HIS327
A	LYS334
A	SER379
A	GLY380
A	GLY381
A	GLY403
A	GLY404
A	MG501
A	HOH661
A	HOH677
A	HOH690
A	HOH698
A	HOH708
A	HOH712
B	GLU60
B	THR65
B	TRP66
B	ASN123
A	THR173
A	LYS175
A	LYS177
A	KCX201
A	ASP203

site_id	AC3
Number of Residues	9
Details	binding site for residue EDO A 503

Chain	Residue
A	GLY111
A	PHE148
A	GLN149
A	THR278
A	HIS282
A	HOH610
A	HOH694
A	HOH777
B	THR246

site_id	AC4
Number of Residues	7
Details	binding site for residue EDO A 504

Chain	Residue
A	THR145
A	LYS146
A	PHE148
A	LEU371
A	HOH770
A	HOH811
B	GLU110

site_id	AC5
Number of Residues	7
Details	binding site for residue EDO A 505

Chain	Residue
A	GLU110
A	HOH783
A	HOH839
B	THR145
B	LYS146
B	PHE148
B	LEU371

site_id	AC6
Number of Residues	8
Details	binding site for residue EDO A 506

Chain	Residue
A	LYS18
A	THR65
A	TRP66
A	THR67
A	THR68
A	EDO509
A	HOH773
A	HOH817

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 507

Chain	Residue
A	LEU270
A	HOH748
A	HOH749
B	LEU270

site_id	AC8
Number of Residues	8
Details	binding site for residue EDO A 508

Chain	Residue
A	GLN304
A	ASN306
A	HIS307
A	HOH646
A	HOH762
B	GLN304
B	ASN306
B	HIS307

site_id	AC9
Number of Residues	7
Details	binding site for residue EDO A 509

Chain	Residue
A	THR65
A	THR67
A	THR68
A	VAL69
A	ASP72
A	EDO506
A	HOH633

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 510

Chain	Residue
A	GLN149
A	ASP286
A	HOH617
A	HOH813

site_id	AD2
Number of Residues	4
Details	binding site for residue MG B 501

Chain	Residue
B	KCX201
B	ASP203
B	GLU204
B	CAP502

site_id	AD3
Number of Residues	28
Details	binding site for residue CAP B 502

Chain	Residue
B	HIS294
B	ARG295
B	HIS327
B	LYS334
B	LEU335
B	SER379
B	GLY380
B	GLY381
B	GLY403
B	GLY404
B	MG501
B	HOH628
B	HOH643
B	HOH665
B	HOH697
B	HOH748
B	HOH765
A	GLU60
A	THR65
A	TRP66
A	ASN123
A	HOH812
B	THR173
B	LYS175
B	LYS177
B	KCX201
B	ASP203
B	GLU204

site_id	AD4
Number of Residues	8
Details	binding site for residue EDO B 503

Chain	Residue
B	LYS18
B	THR65
B	TRP66
B	THR67
B	THR68
B	EDO504
B	HOH708
B	HOH721

site_id	AD5
Number of Residues	9
Details	binding site for residue EDO B 504

Chain	Residue
B	TYR24
B	THR68
B	VAL69
B	ASP72
B	LEU77
B	EDO503
B	HOH708
B	HOH719
B	HOH749

site_id	AD6
Number of Residues	7
Details	binding site for residue EDO B 505

Chain	Residue
B	ASN163
B	TYR165
B	HOH753
J	GLU13
J	ARG100
J	SER114
J	HOH235

site_id	AD7
Number of Residues	6
Details	binding site for residue EDO I 201

Chain	Residue
A	ASN163
A	TYR165
I	GLU13
I	ARG100
I	SER114
I	HOH345

site_id	AD8
Number of Residues	7
Details	binding site for residue EDO I 202

Chain	Residue
A	ASP160
A	ASN163
A	LYS183
A	PHE220
A	GLU223
I	ARG65
I	TYR66

Functional Information from PROSITE/UniProt

site_id	PS00157
Number of Residues	9
Details	RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE

Chain	Residue	Details
A	GLY196-GLU204

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29372894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IU0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"description":"in homodimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29372894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IU0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29372894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IU0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29372894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IU0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29372894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IU0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22092075","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19376835","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)