3NIO
Crystal structure of Pseudomonas aeruginosa guanidinobutyrase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006527 | biological_process | arginine catabolic process |
A | 0008783 | molecular_function | agmatinase activity |
A | 0016787 | molecular_function | hydrolase 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, using agmatinase |
A | 0046872 | molecular_function | metal ion binding |
A | 0047971 | molecular_function | guanidinobutyrase activity |
B | 0006527 | biological_process | arginine catabolic process |
B | 0008783 | molecular_function | agmatinase activity |
B | 0016787 | molecular_function | hydrolase 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, using agmatinase |
B | 0046872 | molecular_function | metal ion binding |
B | 0047971 | molecular_function | guanidinobutyrase activity |
C | 0006527 | biological_process | arginine catabolic process |
C | 0008783 | molecular_function | agmatinase activity |
C | 0016787 | molecular_function | hydrolase 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, using agmatinase |
C | 0046872 | molecular_function | metal ion binding |
C | 0047971 | molecular_function | guanidinobutyrase activity |
D | 0006527 | biological_process | arginine catabolic process |
D | 0008783 | molecular_function | agmatinase activity |
D | 0016787 | molecular_function | hydrolase 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, using agmatinase |
D | 0046872 | molecular_function | metal ion binding |
D | 0047971 | molecular_function | guanidinobutyrase activity |
E | 0006527 | biological_process | arginine catabolic process |
E | 0008783 | molecular_function | agmatinase activity |
E | 0016787 | molecular_function | hydrolase 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, using agmatinase |
E | 0046872 | molecular_function | metal ion binding |
E | 0047971 | molecular_function | guanidinobutyrase activity |
F | 0006527 | biological_process | arginine catabolic process |
F | 0008783 | molecular_function | agmatinase activity |
F | 0016787 | molecular_function | hydrolase 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, using agmatinase |
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: BINDING => ECO:0000255|PROSITE-ProRule:PRU00742, ECO:0000269|PubMed:21600989 |
Chain | Residue | Details |
A | HIS129 | |
B | ASP156 | |
B | ASP243 | |
B | ASP245 | |
C | HIS129 | |
C | ASP152 | |
C | HIS154 | |
C | ASP156 | |
C | ASP243 | |
C | ASP245 | |
D | HIS129 | |
A | ASP152 | |
D | ASP152 | |
D | HIS154 | |
D | ASP156 | |
D | ASP243 | |
D | ASP245 | |
E | HIS129 | |
E | ASP152 | |
E | HIS154 | |
E | ASP156 | |
E | ASP243 | |
A | HIS154 | |
E | ASP245 | |
F | HIS129 | |
F | ASP152 | |
F | HIS154 | |
F | ASP156 | |
F | ASP243 | |
F | ASP245 | |
A | ASP156 | |
A | ASP243 | |
A | ASP245 | |
B | HIS129 | |
B | ASP152 | |
B | HIS154 |