4BOF
Crystal structure of arginine deiminase from group A streptococcus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016990 | molecular_function | arginine deiminase activity |
| A | 0019546 | biological_process | L-arginine deiminase pathway |
| A | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016990 | molecular_function | arginine deiminase activity |
| B | 0019546 | biological_process | L-arginine deiminase pathway |
| B | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006525 | biological_process | arginine metabolic process |
| C | 0006527 | biological_process | L-arginine catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016990 | molecular_function | arginine deiminase activity |
| C | 0019546 | biological_process | L-arginine deiminase pathway |
| C | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006525 | biological_process | arginine metabolic process |
| D | 0006527 | biological_process | L-arginine catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016990 | molecular_function | arginine deiminase activity |
| D | 0019546 | biological_process | L-arginine deiminase pathway |
| D | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006525 | biological_process | arginine metabolic process |
| E | 0006527 | biological_process | L-arginine catabolic process |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016990 | molecular_function | arginine deiminase activity |
| E | 0019546 | biological_process | L-arginine deiminase pathway |
| E | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006525 | biological_process | arginine metabolic process |
| F | 0006527 | biological_process | L-arginine catabolic process |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016990 | molecular_function | arginine deiminase activity |
| F | 0019546 | biological_process | L-arginine deiminase pathway |
| F | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006525 | biological_process | arginine metabolic process |
| G | 0006527 | biological_process | L-arginine catabolic process |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016990 | molecular_function | arginine deiminase activity |
| G | 0019546 | biological_process | L-arginine deiminase pathway |
| G | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006525 | biological_process | arginine metabolic process |
| H | 0006527 | biological_process | L-arginine catabolic process |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0016990 | molecular_function | arginine deiminase activity |
| H | 0019546 | biological_process | L-arginine deiminase pathway |
| H | 0019547 | biological_process | obsolete arginine catabolic process to ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 420 |
| Chain | Residue |
| A | TYR367 |
| A | ASN368 |
| A | ARG369 |
| A | ILE387 |
| A | HIS388 |
| A | GLY389 |
| A | SER390 |
| H | PHE46 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 421 |
| Chain | Residue |
| A | ARG101 |
| A | GLY142 |
| A | THR144 |
| A | ASP145 |
| D | GLU246 |
| A | GLY100 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PGE A 422 |
| Chain | Residue |
| A | LEU71 |
| A | ASN160 |
| A | LEU161 |
| A | PHE163 |
| A | THR164 |
| A | PRO167 |
| A | PHE168 |
| A | ARG185 |
| A | GLU188 |
| A | THR189 |
| A | GLY192 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 420 |
| Chain | Residue |
| B | TYR367 |
| B | ASN368 |
| B | ARG369 |
| B | ILE387 |
| B | HIS388 |
| B | GLY389 |
| B | SER390 |
| C | PHE46 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 421 |
| Chain | Residue |
| B | GLY100 |
| B | ARG101 |
| B | GLY142 |
| B | LEU143 |
| B | THR144 |
| B | ASP145 |
| G | GLU246 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 420 |
| Chain | Residue |
| C | TYR367 |
| C | ASN368 |
| C | ARG369 |
| C | ILE387 |
| C | HIS388 |
| C | GLY389 |
| C | SER390 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 421 |
| Chain | Residue |
| C | GLY100 |
| C | ARG101 |
| C | LEU143 |
| C | THR144 |
| C | ASP145 |
| F | GLU246 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 D 420 |
| Chain | Residue |
| D | TYR367 |
| D | ASN368 |
| D | ARG369 |
| D | ILE387 |
| D | HIS388 |
| D | GLY389 |
| D | SER390 |
| E | PHE46 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 421 |
| Chain | Residue |
| A | GLU246 |
| D | GLY100 |
| D | ARG101 |
| D | GLY142 |
| D | LEU143 |
| D | THR144 |
| D | ASP145 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 E 420 |
| Chain | Residue |
| D | PHE46 |
| E | TYR367 |
| E | ASN368 |
| E | ARG369 |
| E | ILE387 |
| E | HIS388 |
| E | GLY389 |
| E | SER390 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 E 421 |
| Chain | Residue |
| E | GLY100 |
| E | ARG101 |
| E | GLY142 |
| E | LEU143 |
| E | THR144 |
| E | ASP145 |
| H | GLU246 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 F 420 |
| Chain | Residue |
| F | TYR367 |
| F | ASN368 |
| F | ARG369 |
| F | ILE387 |
| F | HIS388 |
| F | GLY389 |
| F | SER390 |
| F | HOH2056 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 F 421 |
| Chain | Residue |
| C | GLU246 |
| F | GLY100 |
| F | ARG101 |
| F | GLY142 |
| F | LEU143 |
| F | THR144 |
| F | ASP145 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PG4 F 422 |
| Chain | Residue |
| F | ASP43 |
| F | ILE44 |
| F | PRO45 |
| F | PHE46 |
| F | LEU47 |
| F | ARG394 |
| F | HOH2062 |
| G | ARG347 |
| G | ASN351 |
| G | ARG369 |
| G | THR371 |
| G | VAL393 |
| G | ARG396 |
| F | GLU29 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE F 423 |
| Chain | Residue |
| F | ALA96 |
| F | ASN97 |
| F | ALA154 |
| F | ASP156 |
| F | PRO157 |
| F | THR184 |
| F | ARG187 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 G 420 |
| Chain | Residue |
| F | HOH2014 |
| G | TYR367 |
| G | ASN368 |
| G | ARG369 |
| G | ILE387 |
| G | HIS388 |
| G | GLY389 |
| G | SER390 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 G 421 |
| Chain | Residue |
| B | GLU246 |
| G | GLY100 |
| G | ARG101 |
| G | GLY142 |
| G | LEU143 |
| G | THR144 |
| G | ASP145 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 H 420 |
| Chain | Residue |
| A | HOH2014 |
| H | TYR367 |
| H | ASN368 |
| H | ARG369 |
| H | ILE387 |
| H | HIS388 |
| H | GLY389 |
| H | SER390 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 H 421 |
| Chain | Residue |
| E | GLU246 |
| H | GLY100 |
| H | ARG101 |
| H | GLY142 |
| H | LEU143 |
| H | THR144 |
| H | ASP145 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Amidino-cysteine intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
