1N2M

The S53A Proenzyme Structure of Methanococcus jannaschii.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006520	biological_process	amino acid metabolic process
A	0006527	biological_process	arginine catabolic process
A	0008792	molecular_function	arginine decarboxylase activity
A	0016831	molecular_function	carboxy-lyase activity
B	0006520	biological_process	amino acid metabolic process
B	0006527	biological_process	arginine catabolic process
B	0008792	molecular_function	arginine decarboxylase activity
B	0016831	molecular_function	carboxy-lyase activity
C	0006520	biological_process	amino acid metabolic process
C	0006527	biological_process	arginine catabolic process
C	0008792	molecular_function	arginine decarboxylase activity
C	0016831	molecular_function	carboxy-lyase activity
D	0006520	biological_process	amino acid metabolic process
D	0006527	biological_process	arginine catabolic process
D	0008792	molecular_function	arginine decarboxylase activity
D	0016831	molecular_function	carboxy-lyase activity
E	0006520	biological_process	amino acid metabolic process
E	0006527	biological_process	arginine catabolic process
E	0008792	molecular_function	arginine decarboxylase activity
E	0016831	molecular_function	carboxy-lyase activity
F	0006520	biological_process	amino acid metabolic process
F	0006527	biological_process	arginine catabolic process
F	0008792	molecular_function	arginine decarboxylase activity
F	0016831	molecular_function	carboxy-lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MRD B 7001

Chain	Residue
A	GLU109
B	PHE34
B	TYR77
B	TYR79
B	ILE81

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MRD F 7002

Chain	Residue
F	TYR79
F	ILE81
D	GLU109
D	HOH6487
F	LEU31
F	TYR77

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MRD D 7003

Chain	Residue
D	LEU31
D	PHE34
D	TYR79
D	ILE81
E	GLU109

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MRD E 7004

Chain	Residue
E	LEU31
E	TYR77
E	TYR79
E	ILE81
F	GLU109

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MRD C 7005

Chain	Residue
B	GLU109
C	LEU31
C	PHE34
C	TYR77
C	TYR79
C	ILE81

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MRD A 7006

Chain	Residue
A	TYR79

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MRD D 7007

Chain	Residue
D	PHE131
D	GLU132
D	GLY135
D	TRP136
F	GLY135
F	TRP136
F	GLU137

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MRD B 7008

Chain	Residue
B	GLU132
B	GLY135
B	TRP136
C	GLY135
C	TRP136
C	GLU137

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	SITE: Cleavage (non-hydrolytic)

Chain	Residue	Details
A	SER52
B	SER52
C	SER52
D	SER52
E	SER52
F	SER52

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:11980912

Chain	Residue	Details
A	ALA53
B	ALA53
C	ALA53
D	ALA53
E	ALA53
F	ALA53

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 707

Chain	Residue	Details
A	ASN47
A	SER52
A	ALA53
A	GLU109	proton shuttle (general acid/base)

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 707

Chain	Residue	Details
B	ASN47
B	SER52
B	ALA53
B	GLU109	proton shuttle (general acid/base)

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 707

Chain	Residue	Details
C	ASN47
C	SER52
C	ALA53
C	GLU109	proton shuttle (general acid/base)

---

site_id	MCSA4
Number of Residues	4
Details	M-CSA 707

Chain	Residue	Details
D	ASN47
D	SER52
D	ALA53
D	GLU109	proton shuttle (general acid/base)

---

site_id	MCSA5
Number of Residues	4
Details	M-CSA 707

Chain	Residue	Details
E	ASN47
E	SER52
E	ALA53
E	GLU109	proton shuttle (general acid/base)

---

site_id	MCSA6
Number of Residues	4
Details	M-CSA 707

Chain	Residue	Details
F	ASN47
F	SER52
F	ALA53
F	GLU109	proton shuttle (general acid/base)

---