1GEH

CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 445

Chain	Residue
A	LYS163
A	GLY369
A	GLN389
A	GLY391
A	GLY392

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 446

Chain	Residue
A	ARG282
A	HIS314

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 1445

Chain	Residue
B	GLN389
B	GLY391
B	GLY392
B	LYS163
B	GLY369

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 1446

Chain	Residue
B	ARG282
B	HIS314

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 2445

Chain	Residue
C	LYS163
C	GLY369
C	GLN389
C	GLY391
C	GLY392

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 2446

Chain	Residue
C	ARG282
C	HIS314

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 3445

Chain	Residue
D	LYS163
D	GLY369
D	GLN389
D	GLY391
D	GLY392

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 3446

Chain	Residue
D	ARG282
D	HIS314

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 4445

Chain	Residue
E	LYS163
E	GLY369
E	GLN389
E	GLY391
E	GLY392

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 E 4446

Chain	Residue
E	ARG282
E	HIS314

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133

Chain	Residue	Details
A	LYS163
E	HIS281
A	HIS281
B	LYS163
B	HIS281
C	LYS163
C	HIS281
D	LYS163
D	HIS281
E	LYS163

---

site_id	SWS_FT_FI2
Number of Residues	25
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS165
B	GLN389
C	LYS165
C	ARG282
C	HIS314
C	SER367
C	GLN389
D	LYS165
D	ARG282
D	HIS314
D	SER367
A	ARG282
D	GLN389
E	LYS165
E	ARG282
E	HIS314
E	SER367
E	GLN389
A	HIS314
A	SER367
A	GLN389
B	LYS165
B	ARG282
B	HIS314
B	SER367

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376

Chain	Residue	Details
A	LYS189
B	LYS189
C	LYS189
D	LYS189
E	LYS189

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376

Chain	Residue	Details
A	ASP191
E	GLU192
A	GLU192
B	ASP191
B	GLU192
C	ASP191
C	GLU192
D	ASP191
D	GLU192
E	ASP191

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01133

Chain	Residue	Details
A	LYS322
B	LYS322
C	LYS322
D	LYS322
E	LYS322

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376

Chain	Residue	Details
A	LYS189
B	LYS189
C	LYS189
D	LYS189
E	LYS189

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS281
A	LYS189
A	HIS314
A	ASP191
A	LYS165
A	LYS163

---

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

Chain	Residue	Details
B	HIS281
B	LYS189
B	HIS314
B	ASP191
B	LYS165
B	LYS163

---

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

Chain	Residue	Details
C	HIS281
C	LYS189
C	HIS314
C	ASP191
C	LYS165
C	LYS163

---

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

Chain	Residue	Details
D	HIS281
D	LYS189
D	HIS314
D	ASP191
D	LYS165
D	LYS163

---

site_id	CSA5
Number of Residues	6
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
E	HIS281
E	LYS189
E	HIS314
E	ASP191
E	LYS165
E	LYS163

---