6VSS
Arginase from Medicago truncatula
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| A | 0004053 | molecular_function | arginase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0008783 | molecular_function | agmatinase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| A | 0034214 | biological_process | protein hexamerization |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000050 | biological_process | urea cycle |
| B | 0004053 | molecular_function | arginase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0008783 | molecular_function | agmatinase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| B | 0034214 | biological_process | protein hexamerization |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000050 | biological_process | urea cycle |
| C | 0004053 | molecular_function | arginase activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0008783 | molecular_function | agmatinase activity |
| C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| C | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| C | 0034214 | biological_process | protein hexamerization |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000050 | biological_process | urea cycle |
| D | 0004053 | molecular_function | arginase activity |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0008783 | molecular_function | agmatinase activity |
| D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| D | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| D | 0034214 | biological_process | protein hexamerization |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000050 | biological_process | urea cycle |
| E | 0004053 | molecular_function | arginase activity |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0008783 | molecular_function | agmatinase activity |
| E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| E | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| E | 0034214 | biological_process | protein hexamerization |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000050 | biological_process | urea cycle |
| F | 0004053 | molecular_function | arginase activity |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0008783 | molecular_function | agmatinase activity |
| F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| F | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| F | 0034214 | biological_process | protein hexamerization |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue MN A 401 |
| Chain | Residue |
| A | ASP181 |
| A | HIS183 |
| A | ASP266 |
| A | ASP268 |
| A | MN402 |
| A | HOH512 |
| A | HOH584 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MN A 402 |
| Chain | Residue |
| A | ASP185 |
| A | ASP266 |
| A | MN401 |
| A | HOH512 |
| A | HOH584 |
| A | HIS157 |
| A | ASP181 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 401 |
| Chain | Residue |
| B | ASP181 |
| B | HIS183 |
| B | ASP266 |
| B | ASP268 |
| B | MN402 |
| B | HOH534 |
| B | HOH584 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 402 |
| Chain | Residue |
| B | HIS157 |
| B | ASP181 |
| B | ASP185 |
| B | ASP266 |
| B | MN401 |
| B | HOH534 |
| B | HOH584 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MN C 401 |
| Chain | Residue |
| C | ASP181 |
| C | HIS183 |
| C | ASP266 |
| C | ASP268 |
| C | MN402 |
| C | HOH512 |
| C | HOH560 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 402 |
| Chain | Residue |
| C | HIS157 |
| C | ASP181 |
| C | ASP185 |
| C | ASP266 |
| C | MN401 |
| C | HOH512 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MN D 401 |
| Chain | Residue |
| D | ASP181 |
| D | HIS183 |
| D | ASP266 |
| D | ASP268 |
| D | MN402 |
| D | HOH505 |
| D | HOH569 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MN D 402 |
| Chain | Residue |
| D | HIS157 |
| D | ASP181 |
| D | ASP185 |
| D | ASP266 |
| D | MN401 |
| D | HOH505 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MN E 401 |
| Chain | Residue |
| E | ASP181 |
| E | HIS183 |
| E | ASP266 |
| E | ASP268 |
| E | MN402 |
| E | HOH510 |
| E | HOH570 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue MN E 402 |
| Chain | Residue |
| E | HIS157 |
| E | ASP181 |
| E | ASP185 |
| E | ASP266 |
| E | MN401 |
| E | HOH510 |
| E | HOH570 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MN F 401 |
| Chain | Residue |
| F | ASP181 |
| F | HIS183 |
| F | ASP266 |
| F | ASP268 |
| F | MN402 |
| F | HOH547 |
| F | HOH567 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MN F 402 |
| Chain | Residue |
| F | HIS157 |
| F | ASP181 |
| F | ASP185 |
| F | ASP266 |
| F | MN401 |
| F | HOH547 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SIDVDsldPsiaPGvshhepgG |
| Chain | Residue | Details |
| A | SER264-GLY285 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32754173","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32754173","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P53608","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32754173","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






