Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5HQL

Structure function studies of R. palustris RubisCO (A47V-M331A mutant; CABP-bound; no expression tag)

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	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
B	0000287	molecular_function	magnesium ion binding
B	0004497	molecular_function	monooxygenase activity
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	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	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
D	0000287	molecular_function	magnesium ion binding
D	0004497	molecular_function	monooxygenase activity
D	0015977	biological_process	carbon fixation
D	0015979	biological_process	photosynthesis
D	0016491	molecular_function	oxidoreductase activity
D	0016829	molecular_function	lyase activity
D	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
D	0019253	biological_process	reductive pentose-phosphate cycle
D	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	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
F	0000287	molecular_function	magnesium ion binding
F	0004497	molecular_function	monooxygenase activity
F	0015977	biological_process	carbon fixation
F	0015979	biological_process	photosynthesis
F	0016491	molecular_function	oxidoreductase activity
F	0016829	molecular_function	lyase activity
F	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
F	0019253	biological_process	reductive pentose-phosphate cycle
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue CAP A 500

Chain	Residue
A	ILE165
A	LYS330
A	SER369
A	GLY370
A	GLY371
A	GLY394
A	GLY395
A	MG501
A	HOH623
A	HOH635
B	GLU49
A	LYS167
B	THR54
B	ASN112
A	LYS169
A	KCX192
A	ASP194
A	GLU195
A	HIS288
A	ARG289
A	HIS322

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 501

Chain	Residue
A	LYS169
A	KCX192
A	ASP194
A	GLU195
A	CAP500
B	ASN112

site_id	AC3
Number of Residues	23
Details	binding site for residue CAP B 500

Chain	Residue
A	GLU49
A	THR54
A	ASN112
B	ILE165
B	LYS167
B	LYS169
B	KCX192
B	ASP194
B	GLU195
B	HIS288
B	ARG289
B	HIS322
B	LYS330
B	SER369
B	GLY370
B	GLY371
B	ALA393
B	GLY394
B	GLY395
B	MG501
B	HOH606
B	HOH624
B	HOH642

site_id	AC4
Number of Residues	6
Details	binding site for residue MG B 501

Chain	Residue
B	LYS167
B	LYS169
B	KCX192
B	ASP194
B	GLU195
B	CAP500

site_id	AC5
Number of Residues	21
Details	binding site for residue CAP C 500

Chain	Residue
C	ILE165
C	LYS167
C	LYS169
C	KCX192
C	ASP194
C	GLU195
C	HIS288
C	ARG289
C	HIS322
C	LYS330
C	SER369
C	GLY370
C	GLY371
C	GLY394
C	GLY395
C	MG501
C	HOH613
C	HOH621
E	GLU49
E	THR54
E	ASN112

site_id	AC6
Number of Residues	4
Details	binding site for residue MG C 501

Chain	Residue
C	KCX192
C	ASP194
C	GLU195
C	CAP500

site_id	AC7
Number of Residues	21
Details	binding site for residue CAP D 500

Chain	Residue
F	GLU49
F	THR54
F	ASN112
D	ILE165
D	LYS167
D	LYS169
D	KCX192
D	ASP194
D	GLU195
D	HIS288
D	ARG289
D	HIS322
D	LYS330
D	SER369
D	GLY370
D	GLY371
D	ALA393
D	GLY394
D	GLY395
D	MG501
D	HOH619

site_id	AC8
Number of Residues	5
Details	binding site for residue MG D 501

Chain	Residue
D	LYS169
D	KCX192
D	ASP194
D	GLU195
D	CAP500

site_id	AC9
Number of Residues	22
Details	binding site for residue CAP E 500

Chain	Residue
C	GLU49
C	THR54
C	ASN112
E	ILE165
E	LYS167
E	LYS169
E	KCX192
E	ASP194
E	GLU195
E	HIS288
E	ARG289
E	HIS322
E	LYS330
E	SER369
E	GLY370
E	GLY371
E	ALA393
E	GLY394
E	GLY395
E	MG501
E	HOH611
E	HOH641

site_id	AD1
Number of Residues	5
Details	binding site for residue MG E 501

Chain	Residue
E	LYS169
E	KCX192
E	ASP194
E	GLU195
E	CAP500

site_id	AD2
Number of Residues	21
Details	binding site for residue CAP F 500

Chain	Residue
D	GLU49
D	THR54
D	ASN112
F	ILE165
F	LYS167
F	LYS169
F	KCX192
F	ASP194
F	GLU195
F	HIS288
F	ARG289
F	HIS292
F	HIS322
F	LYS330
F	SER369
F	GLY370
F	GLY371
F	GLY394
F	GLY395
F	MG501
F	HOH612

site_id	AD3
Number of Residues	7
Details	binding site for residue MG F 501

Chain	Residue
D	ASN112
F	LYS169
F	KCX192
F	ASP194
F	GLU195
F	HIS288
F	CAP500

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY187-GLU195

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"description":"in homodimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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