3NIO
Crystal structure of Pseudomonas aeruginosa guanidinobutyrase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0008783 | molecular_function | agmatinase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047971 | molecular_function | guanidinobutyrase activity |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0008783 | molecular_function | agmatinase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047971 | molecular_function | guanidinobutyrase activity |
| C | 0006527 | biological_process | L-arginine catabolic process |
| C | 0008783 | molecular_function | agmatinase activity |
| C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| C | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047971 | molecular_function | guanidinobutyrase activity |
| D | 0006527 | biological_process | L-arginine catabolic process |
| D | 0008783 | molecular_function | agmatinase activity |
| D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| D | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047971 | molecular_function | guanidinobutyrase activity |
| E | 0006527 | biological_process | L-arginine catabolic process |
| E | 0008783 | molecular_function | agmatinase activity |
| E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| E | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047971 | molecular_function | guanidinobutyrase activity |
| F | 0006527 | biological_process | L-arginine catabolic process |
| F | 0008783 | molecular_function | agmatinase activity |
| F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| F | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0047971 | molecular_function | guanidinobutyrase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN A 1601 |
| Chain | Residue |
| A | HIS129 |
| A | ASP152 |
| A | ASP156 |
| A | ASP243 |
| A | HOH624 |
| A | HOH1061 |
| A | MN1602 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 1602 |
| Chain | Residue |
| A | ASP243 |
| A | ASP245 |
| A | HOH624 |
| A | MN1601 |
| A | ASP152 |
| A | HIS154 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 1603 |
| Chain | Residue |
| B | HIS129 |
| B | ASP152 |
| B | ASP156 |
| B | ASP243 |
| B | HOH791 |
| B | HOH1060 |
| B | MN1604 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 1604 |
| Chain | Residue |
| B | ASP152 |
| B | HIS154 |
| B | ASP243 |
| B | ASP245 |
| B | HOH791 |
| B | MN1603 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN C 1605 |
| Chain | Residue |
| C | HIS129 |
| C | ASP152 |
| C | ASP156 |
| C | ASP243 |
| C | HOH1007 |
| C | HOH1059 |
| C | MN1606 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 1606 |
| Chain | Residue |
| C | ASP152 |
| C | HIS154 |
| C | ASP243 |
| C | ASP245 |
| C | HOH1007 |
| C | MN1605 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN D 1607 |
| Chain | Residue |
| D | HIS129 |
| D | ASP152 |
| D | ASP156 |
| D | ASP243 |
| D | HOH1040 |
| D | HOH1058 |
| D | MN1608 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 1608 |
| Chain | Residue |
| D | ASP152 |
| D | HIS154 |
| D | ASP243 |
| D | ASP245 |
| D | HOH1040 |
| D | MN1607 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN E 1609 |
| Chain | Residue |
| E | HIS129 |
| E | ASP152 |
| E | ASP156 |
| E | ASP243 |
| E | HOH1033 |
| E | HOH1057 |
| E | MN1610 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN E 1610 |
| Chain | Residue |
| E | ASP152 |
| E | HIS154 |
| E | ASP243 |
| E | ASP245 |
| E | HOH1033 |
| E | MN1609 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN F 1611 |
| Chain | Residue |
| F | HIS129 |
| F | ASP152 |
| F | ASP156 |
| F | ASP243 |
| F | HOH1034 |
| F | HOH1056 |
| F | MN1612 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN F 1612 |
| Chain | Residue |
| F | ASP152 |
| F | HIS154 |
| F | ASP243 |
| F | ASP245 |
| F | HOH1034 |
| F | MN1611 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SFDIDgidPawaPGtgtpeigG |
| Chain | Residue | Details |
| A | SER241-GLY262 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21600989","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
