1MT1
The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from 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 |
G | 0006520 | biological_process | amino acid metabolic process |
G | 0006527 | biological_process | arginine catabolic process |
G | 0008792 | molecular_function | arginine decarboxylase activity |
G | 0016831 | molecular_function | carboxy-lyase activity |
H | 0006520 | biological_process | amino acid metabolic process |
H | 0006527 | biological_process | arginine catabolic process |
H | 0008792 | molecular_function | arginine decarboxylase activity |
H | 0016831 | molecular_function | carboxy-lyase activity |
I | 0006520 | biological_process | amino acid metabolic process |
I | 0006527 | biological_process | arginine catabolic process |
I | 0008792 | molecular_function | arginine decarboxylase activity |
I | 0016831 | molecular_function | carboxy-lyase activity |
J | 0006520 | biological_process | amino acid metabolic process |
J | 0006527 | biological_process | arginine catabolic process |
J | 0008792 | molecular_function | arginine decarboxylase activity |
J | 0016831 | molecular_function | carboxy-lyase activity |
K | 0006520 | biological_process | amino acid metabolic process |
K | 0006527 | biological_process | arginine catabolic process |
K | 0008792 | molecular_function | arginine decarboxylase activity |
K | 0016831 | molecular_function | carboxy-lyase activity |
L | 0006520 | biological_process | amino acid metabolic process |
L | 0006527 | biological_process | arginine catabolic process |
L | 0008792 | molecular_function | arginine decarboxylase activity |
L | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AG2 B 7001 |
Chain | Residue |
A | SER52 |
C | VAL46 |
B | PYR53 |
B | ILE107 |
B | MSE108 |
B | GLU109 |
C | LEU31 |
C | ASP35 |
C | LEU38 |
C | GLY44 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AG2 K 7002 |
Chain | Residue |
G | SER52 |
H | PYR53 |
H | ILE107 |
H | GLU109 |
K | LEU31 |
K | ASP35 |
K | LEU38 |
K | GLY44 |
K | VAL46 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AG2 G 7003 |
Chain | Residue |
G | LEU31 |
G | ASP35 |
G | LEU38 |
G | GLY44 |
G | VAL46 |
I | SER52 |
J | PYR53 |
J | ILE107 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AG2 C 7004 |
Chain | Residue |
C | SER52 |
D | PYR53 |
D | ILE107 |
E | LEU31 |
E | ASP35 |
E | LEU38 |
E | VAL46 |
E | HOH71 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AG2 A 7005 |
Chain | Residue |
A | ASP35 |
A | LEU38 |
A | GLY44 |
A | VAL46 |
E | SER52 |
F | PYR53 |
F | ILE107 |
F | GLU109 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | SITE: Cleavage (non-hydrolytic) |
Chain | Residue | Details |
A | SER52 | |
C | SER52 | |
E | SER52 | |
G | SER52 | |
I | SER52 | |
K | SER52 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
B | GLU109 |
site_id | CSA2 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
D | GLU109 |
site_id | CSA3 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
F | GLU109 |
site_id | CSA4 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
H | GLU109 |
site_id | CSA5 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
J | GLU109 |
site_id | CSA6 |
Number of Residues | 1 |
Details |
Chain | Residue | Details |
L | GLU109 |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 707 |
Chain | Residue | Details |
B | GLU109 | proton shuttle (general acid/base) |
A | SER52 |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 707 |
Chain | Residue | Details |
D | GLU109 | proton shuttle (general acid/base) |
C | SER52 |
site_id | MCSA3 |
Number of Residues | 1 |
Details | M-CSA 707 |
Chain | Residue | Details |
F | GLU109 | proton shuttle (general acid/base) |
E | SER52 |
site_id | MCSA4 |
Number of Residues | 1 |
Details | M-CSA 707 |
Chain | Residue | Details |
H | GLU109 | proton shuttle (general acid/base) |
G | SER52 |
site_id | MCSA5 |
Number of Residues | 1 |
Details | M-CSA 707 |
Chain | Residue | Details |
J | GLU109 | proton shuttle (general acid/base) |
I | SER52 |
site_id | MCSA6 |
Number of Residues | 1 |
Details | M-CSA 707 |
Chain | Residue | Details |
L | GLU109 | proton shuttle (general acid/base) |
K | SER52 |