Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1AUS

ACTIVATED UNLIGANDED SPINACH RUBISCO

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG L 476

Chain	Residue
L	ASP203
L	GLU204
L	FMT477
L	HOH570
L	HOH588
L	HOH623

site_id	AC2
Number of Residues	4
Details

Chain	Residue
L	LYS201
L	ASP203
L	GLU204
M	MG476

site_id	AC3
Number of Residues	4
Details

Chain	Residue
L	ASP203
L	GLU204
N	MG476
L	LYS201

site_id	AC4
Number of Residues	4
Details

Chain	Residue
L	LYS201
L	ASP203
L	GLU204
O	MG476

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG M 476

Chain	Residue
M	ASP203
M	GLU204
M	FMT477

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG N 476

Chain	Residue
N	ASP203
N	GLU204
N	FMT477

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG O 476

Chain	Residue
O	ASP203
O	GLU204
O	FMT477

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FMT L 477

Chain	Residue
L	THR173
L	LYS201
L	ASP203
L	GLU204
L	HIS294
L	HIS327
L	MG476
L	HOH588
L	HOH653

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT M 477

Chain	Residue
M	THR173
M	LYS201
M	ASP203
M	GLU204
M	HIS294
M	HIS327
M	MG476

site_id	ACT
Number of Residues	4
Details	CATALYTIC RESIDUES

Chain	Residue
L	LYS201
L	ASP203
L	GLU204
L	MG476

site_id	AD1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT N 477

Chain	Residue
N	THR173
N	LYS201
N	ASP203
N	GLU204
N	HIS294
N	HIS327
N	MG476

site_id	AD2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT O 477

Chain	Residue
O	THR173
O	LYS201
O	ASP203
O	GLU204
O	HIS294
O	HIS327
O	MG476

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
L	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	16
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	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	6
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
L	LYS175
L	LYS201
L	LYS177
L	HIS294
L	ASP203
L	HIS327

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
M	LYS175
M	LYS201
M	LYS177
M	HIS294
M	ASP203
M	HIS327

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
N	LYS175
N	LYS201
N	LYS177
N	HIS294
N	ASP203
N	HIS327

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
O	LYS175
O	LYS201
O	LYS177
O	HIS294
O	ASP203
O	HIS327

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