Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1BXN

THE CRYSTAL STRUCTURE OF RUBISCO FROM ALCALIGENES EUTROPHUS TO 2.7 ANGSTROMS.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004497	molecular_function	monooxygenase activity
A	0015977	biological_process	carbon fixation
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	0015977	biological_process	carbon fixation
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	0015977	biological_process	carbon fixation
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	0015977	biological_process	carbon fixation
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
I	0015977	biological_process	carbon fixation
I	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
I	0019253	biological_process	reductive pentose-phosphate cycle
J	0015977	biological_process	carbon fixation
J	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
J	0019253	biological_process	reductive pentose-phosphate cycle
K	0015977	biological_process	carbon fixation
K	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
K	0019253	biological_process	reductive pentose-phosphate cycle
L	0015977	biological_process	carbon fixation
L	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
L	0019253	biological_process	reductive pentose-phosphate cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 501

Chain	Residue
A	ARG297
A	HIS329
A	GLU338
A	SER381
E	ASN126

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 502

Chain	Residue
E	TRP69
A	GLY382
A	GLY405
A	GLY406
E	THR68

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 503

Chain	Residue
C	ARG297
C	HIS329
C	GLU338
C	SER381

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 C 504

Chain	Residue
C	THR68
C	TRP69
C	GLY382
C	GLY383
C	GLY405
C	GLY406

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 505

Chain	Residue
E	ARG297
E	HIS329
E	GLU338
E	SER381

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 506

Chain	Residue
A	THR68
A	TRP69
E	GLY382
E	GLY405
E	GLY406

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 G 507

Chain	Residue
G	ARG297
G	HIS329
G	GLU338
G	SER381

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 G 508

Chain	Residue
G	THR68
G	TRP69
G	GLY405
G	GLY406

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY199-GLU207

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	PRO179
A	ARG297
C	PRO179
C	ARG297
E	PRO179
E	ARG297
G	PRO179
G	ARG297

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: in homodimeric partner

Chain	Residue	Details
A	VAL127
C	VAL127
E	VAL127
G	VAL127

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING:

Chain	Residue	Details
A	THR177
C	GLU207
C	ASN208
C	ALA298
C	THR330
C	GLY382
E	THR177
E	LEU181
E	GLU207
E	ASN208
E	ALA298
A	LEU181
E	THR330
E	GLY382
G	THR177
G	LEU181
G	GLU207
G	ASN208
G	ALA298
G	THR330
G	GLY382
A	GLU207
A	ASN208
A	ALA298
A	THR330
A	GLY382
C	THR177
C	LEU181

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: via carbamate group

Chain	Residue	Details
A	ASP205
C	ASP205
E	ASP205
G	ASP205

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	LEU337
C	LEU337
E	LEU337
G	LEU337

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:2820933

Chain	Residue	Details
A	ASP205
C	ASP205
E	ASP205
G	ASP205

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
A	LYS204
A	ASP206
A	LYS180
A	HIS329
A	HIS296
A	LYS178

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

Chain	Residue	Details
C	LYS204
C	ASP206
C	LYS180
C	HIS329
C	HIS296
C	LYS178

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

Chain	Residue	Details
E	LYS204
E	ASP206
E	LYS180
E	HIS329
E	HIS296
E	LYS178

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

Chain	Residue	Details
G	LYS204
G	ASP206
G	LYS180
G	HIS329
G	HIS296
G	LYS178

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