Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3A13

Crystal structure of Type III Rubisco SP4 mutant complexed with 2-CABP and activated with Ca

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0006196	biological_process	AMP catabolic process
A	0015977	biological_process	carbon fixation
A	0016491	molecular_function	oxidoreductase activity
A	0016829	molecular_function	lyase activity
A	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0006196	biological_process	AMP catabolic process
B	0015977	biological_process	carbon fixation
B	0016491	molecular_function	oxidoreductase activity
B	0016829	molecular_function	lyase activity
B	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0006196	biological_process	AMP catabolic process
C	0015977	biological_process	carbon fixation
C	0016491	molecular_function	oxidoreductase activity
C	0016829	molecular_function	lyase activity
C	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0006196	biological_process	AMP catabolic process
D	0015977	biological_process	carbon fixation
D	0016491	molecular_function	oxidoreductase activity
D	0016829	molecular_function	lyase activity
D	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0006196	biological_process	AMP catabolic process
E	0015977	biological_process	carbon fixation
E	0016491	molecular_function	oxidoreductase activity
E	0016829	molecular_function	lyase activity
E	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0006196	biological_process	AMP catabolic process
F	0015977	biological_process	carbon fixation
F	0016491	molecular_function	oxidoreductase activity
F	0016829	molecular_function	lyase activity
F	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
F	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0006196	biological_process	AMP catabolic process
G	0015977	biological_process	carbon fixation
G	0016491	molecular_function	oxidoreductase activity
G	0016829	molecular_function	lyase activity
G	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
G	0046872	molecular_function	metal ion binding
H	0000287	molecular_function	magnesium ion binding
H	0006196	biological_process	AMP catabolic process
H	0015977	biological_process	carbon fixation
H	0016491	molecular_function	oxidoreductase activity
H	0016829	molecular_function	lyase activity
H	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
H	0046872	molecular_function	metal ion binding
I	0000287	molecular_function	magnesium ion binding
I	0006196	biological_process	AMP catabolic process
I	0015977	biological_process	carbon fixation
I	0016491	molecular_function	oxidoreductase activity
I	0016829	molecular_function	lyase activity
I	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
I	0046872	molecular_function	metal ion binding
J	0000287	molecular_function	magnesium ion binding
J	0006196	biological_process	AMP catabolic process
J	0015977	biological_process	carbon fixation
J	0016491	molecular_function	oxidoreductase activity
J	0016829	molecular_function	lyase activity
J	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
J	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 445

Chain	Residue
A	KCX189
A	ASP191
A	GLU192
A	CAP446

site_id	AC2
Number of Residues	29
Details	BINDING SITE FOR RESIDUE CAP A 446

Chain	Residue
A	HIS281
A	ARG282
A	HIS314
A	LYS322
A	LEU323
A	SER367
A	GLY368
A	GLY369
A	GLN389
A	GLY391
A	GLY392
A	MG445
A	HOH508
A	HOH523
A	HOH528
A	HOH529
A	HOH535
A	HOH554
A	HOH584
A	HOH625
C	GLU49
C	THR54
C	TRP55
C	ASN111
A	LYS163
A	LYS165
A	KCX189
A	ASP191
A	GLU192

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 445

Chain	Residue
B	ASN111
B	LYS163
B	LYS165
B	KCX189
B	ASP191
B	GLU192
B	CAP446

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE CAP B 446

Chain	Residue
B	GLU49
B	TRP55
B	ASN111
B	LYS163
B	LYS165
B	KCX189
B	ASP191
B	GLU192
B	HIS281
B	ARG282
B	HIS314
B	LYS322
B	LEU323
B	SER367
B	GLY368
B	GLY369
B	GLN389
B	GLY391
B	GLY392
B	MG445
B	HOH510
B	HOH516
B	HOH520
B	HOH534
B	HOH554
B	HOH555
B	HOH667

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 445

Chain	Residue
C	LYS163
C	KCX189
C	ASP191
C	GLU192
C	CAP446

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE CAP C 446

Chain	Residue
A	GLU49
A	TRP55
A	ASN111
C	LYS163
C	LYS165
C	KCX189
C	GLU192
C	HIS281
C	ARG282
C	HIS314
C	LYS322
C	LEU323
C	SER367
C	GLY368
C	GLY369
C	GLN389
C	GLY391
C	GLY392
C	MG445
C	HOH518
C	HOH522
C	HOH536
C	HOH553
C	HOH586
C	HOH661

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 445

Chain	Residue
D	GLU192
D	CAP446
D	KCX189
D	ASP191

site_id	AC8
Number of Residues	26
Details	BINDING SITE FOR RESIDUE CAP D 446

Chain	Residue
D	LYS163
D	LYS165
D	KCX189
D	ASP191
D	GLU192
D	HIS281
D	ARG282
D	HIS314
D	LYS322
D	SER367
D	GLY368
D	GLY369
D	GLN389
D	GLY391
D	GLY392
D	MG445
D	HOH504
D	HOH521
D	HOH532
D	HOH536
D	HOH601
D	HOH710
E	GLU49
E	THR54
E	TRP55
E	ASN111

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 445

Chain	Residue
E	KCX189
E	ASP191
E	GLU192
E	CAP446
E	HOH666

site_id	BC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE CAP E 446

Chain	Residue
D	TRP55
D	ASN111
E	KCX189
E	GLU192
E	HIS281
E	ARG282
E	HIS314
E	SER367
E	GLY368
E	GLY369
E	GLN389
E	LEU390
E	GLY391
E	GLY392
E	CA445
E	HOH528
E	HOH535
E	HOH556
E	HOH577
E	HOH627
E	HOH666
E	HOH687

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 445

Chain	Residue
F	KCX189
F	ASP191
F	GLU192
F	CAP446

site_id	BC3
Number of Residues	28
Details	BINDING SITE FOR RESIDUE CAP F 446

Chain	Residue
F	LYS163
F	LYS165
F	KCX189
F	ASP191
F	GLU192
F	HIS281
F	ARG282
F	HIS314
F	LYS322
F	LEU323
F	SER367
F	GLY368
F	GLY369
F	GLN389
F	GLY391
F	GLY392
F	MG445
F	HOH520
F	HOH524
F	HOH528
F	HOH541
F	HOH562
F	HOH570
F	HOH623
H	GLU49
H	THR54
H	TRP55
H	ASN111

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 445

Chain	Residue
G	LYS163
G	LYS165
G	KCX189
G	ASP191
G	GLU192
G	CAP446

site_id	BC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE CAP G 446

Chain	Residue
G	GLU49
G	TRP55
G	ASN111
G	LYS163
G	LYS165
G	KCX189
G	ASP191
G	GLU192
G	HIS281
G	ARG282
G	HIS314
G	LYS322
G	LEU323
G	SER367
G	GLY368
G	GLY369
G	GLN389
G	GLY391
G	GLY392
G	MG445
G	HOH503
G	HOH528
G	HOH536
G	HOH582
G	HOH603
G	HOH669
G	HOH672

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG H 445

Chain	Residue
H	LYS165
H	KCX189
H	ASP191
H	GLU192
H	CAP446

site_id	BC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE CAP H 446

Chain	Residue
F	TRP55
F	ASN111
F	HOH519
H	LYS163
H	LYS165
H	KCX189
H	GLU192
H	HIS281
H	ARG282
H	HIS314
H	LYS322
H	LEU323
H	SER367
H	GLY368
H	GLY369
H	GLN389
H	GLY391
H	GLY392
H	MG445
H	HOH535
H	HOH543
H	HOH607
H	HOH652

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG I 445

Chain	Residue
I	LYS163
I	KCX189
I	ASP191
I	GLU192
I	CAP446

site_id	BC9
Number of Residues	28
Details	BINDING SITE FOR RESIDUE CAP I 446

Chain	Residue
I	LYS163
I	LYS165
I	KCX189
I	ASP191
I	GLU192
I	HIS281
I	ARG282
I	HIS314
I	LYS322
I	LEU323
I	SER367
I	GLY368
I	GLY369
I	GLN389
I	GLY391
I	GLY392
I	MG445
I	HOH536
I	HOH537
I	HOH543
I	HOH547
I	HOH575
I	HOH659
I	HOH673
J	GLU49
J	THR54
J	TRP55
J	ASN111

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA J 445

Chain	Residue
J	KCX189
J	ASP191
J	GLU192
J	CAP446
J	HOH678

site_id	CC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE CAP J 446

Chain	Residue
I	TRP55
I	ASN111
J	KCX189
J	GLU192
J	HIS281
J	ARG282
J	HIS314
J	SER367
J	GLY368
J	GLY369
J	GLN389
J	LEU390
J	GLY391
J	GLY392
J	CA445
J	HOH526
J	HOH538
J	HOH547
J	HOH549
J	HOH586
J	HOH604
J	HOH678

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	78
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20926376","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20926376","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	10
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	10
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20926376","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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