Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1UPP

SPINACH RUBISCO IN COMPLEX WITH 2-CARBOXYARABINITOL 2 BISPHOSPHATE and Calcium.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004497	molecular_function	monooxygenase activity
A	0009507	cellular_component	chloroplast
A	0009853	biological_process	photorespiration
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	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004497	molecular_function	monooxygenase activity
C	0009507	cellular_component	chloroplast
C	0009853	biological_process	photorespiration
C	0015977	biological_process	carbon fixation
C	0015979	biological_process	photosynthesis
C	0016491	molecular_function	oxidoreductase activity
C	0016829	molecular_function	lyase activity
C	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
C	0019253	biological_process	reductive pentose-phosphate cycle
C	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0004497	molecular_function	monooxygenase activity
E	0009507	cellular_component	chloroplast
E	0009853	biological_process	photorespiration
E	0015977	biological_process	carbon fixation
E	0015979	biological_process	photosynthesis
E	0016491	molecular_function	oxidoreductase activity
E	0016829	molecular_function	lyase activity
E	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
E	0019253	biological_process	reductive pentose-phosphate cycle
E	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0004497	molecular_function	monooxygenase activity
G	0009507	cellular_component	chloroplast
G	0009853	biological_process	photorespiration
G	0015977	biological_process	carbon fixation
G	0015979	biological_process	photosynthesis
G	0016491	molecular_function	oxidoreductase activity
G	0016829	molecular_function	lyase activity
G	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
G	0019253	biological_process	reductive pentose-phosphate cycle
G	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 476

Chain	Residue
A	LYS175
A	LYS177
A	KCX201
A	ASP203
A	GLU204
A	CAP477

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 476

Chain	Residue
C	ASP203
C	GLU204
C	CAP477
C	LYS175
C	LYS177
C	KCX201

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 476

Chain	Residue
E	LYS177
E	KCX201
E	ASP203
E	GLU204
E	CAP477

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA G 476

Chain	Residue
G	LYS177
G	KCX201
G	ASP203
G	GLU204
G	CAP477

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE CAP A 477

Chain	Residue
A	THR173
A	LYS175
A	LYS177
A	KCX201
A	GLU204
A	HIS294
A	ARG295
A	HIS327
A	LYS334
A	LEU335
A	SER379
A	GLY380
A	GLY381
A	GLY403
A	GLY404
A	CA476
A	HOH2070
A	HOH2110
A	HOH2111
A	HOH2112
E	GLU60
E	THR65
E	TRP66
E	ASN123
E	HOH2016

site_id	AC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE CAP C 477

Chain	Residue
C	GLU60
C	THR65
C	TRP66
C	ASN123
C	THR173
C	LYS175
C	LYS177
C	KCX201
C	HIS294
C	ARG295
C	HIS327
C	LYS334
C	LEU335
C	SER379
C	GLY380
C	GLY381
C	PHE402
C	GLY403
C	GLY404
C	CA476
C	HOH2082
C	HOH2083
C	HOH2105
C	HOH2108

site_id	AC7
Number of Residues	25
Details	BINDING SITE FOR RESIDUE CAP E 477

Chain	Residue
A	GLU60
A	THR65
A	TRP66
A	ASN123
E	THR173
E	LYS175
E	LYS177
E	KCX201
E	HIS294
E	ARG295
E	HIS327
E	LYS334
E	LEU335
E	SER379
E	GLY380
E	GLY381
E	GLY403
E	GLY404
E	CA476
E	HOH2080
E	HOH2081
E	HOH2129
E	HOH2130
E	HOH2131
E	HOH2132

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE CAP G 477

Chain	Residue
G	ASN123
G	THR173
G	LYS175
G	LYS177
G	KCX201
G	HIS294
G	ARG295
G	HIS327
G	LYS334
G	LEU335
G	SER379
G	GLY380
G	GLY381
G	GLY403
G	GLY404
G	CA476
G	HOH2088
G	HOH2104
G	HOH2132
G	HOH2133
G	GLU60
G	THR65
G	TRP66

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":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"description":"in homodimeric partner","evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Site: {"description":"Not N6-methylated","evidences":[{"source":"PubMed","id":"2928307","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8955130","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
A	LYS175
A	HIS294
A	LYS177
A	ASP203
A	HIS327

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
C	LYS175
C	HIS294
C	LYS177
C	ASP203
C	HIS327

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
E	LYS175
E	HIS294
E	LYS177
E	ASP203
E	HIS327

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
G	LYS175
G	HIS294
G	LYS177
G	ASP203
G	HIS327

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