1PQ3
Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004053 | molecular_function | arginase activity |
A | 0006525 | biological_process | arginine metabolic process |
A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
A | 0046872 | molecular_function | metal ion binding |
B | 0004053 | molecular_function | arginase activity |
B | 0006525 | biological_process | arginine metabolic process |
B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
B | 0046872 | molecular_function | metal ion binding |
C | 0004053 | molecular_function | arginase activity |
C | 0006525 | biological_process | arginine metabolic process |
C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
C | 0046872 | molecular_function | metal ion binding |
D | 0004053 | molecular_function | arginase activity |
D | 0006525 | biological_process | arginine metabolic process |
D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
D | 0046872 | molecular_function | metal ion binding |
E | 0004053 | molecular_function | arginase activity |
E | 0006525 | biological_process | arginine metabolic process |
E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
E | 0046872 | molecular_function | metal ion binding |
F | 0004053 | molecular_function | arginase activity |
F | 0006525 | biological_process | arginine metabolic process |
F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 3070 |
Chain | Residue |
A | ARG220 |
A | ARG224 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 3071 |
Chain | Residue |
F | ARG220 |
F | ASP221 |
F | ARG224 |
F | HOH973 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 3072 |
Chain | Residue |
D | ARG220 |
D | ARG224 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 3073 |
Chain | Residue |
A | ARG233 |
A | ARG224 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 F 3074 |
Chain | Residue |
F | ARG224 |
F | LEU225 |
F | ARG233 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 3075 |
Chain | Residue |
C | ARG220 |
C | ARG224 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 3077 |
Chain | Residue |
F | PRO179 |
F | GLY180 |
F | PHE181 |
F | SER182 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 3078 |
Chain | Residue |
C | PRO179 |
C | GLY180 |
C | PHE181 |
C | SER182 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 3079 |
Chain | Residue |
D | GLY180 |
D | PHE181 |
D | SER182 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 3080 |
Chain | Residue |
D | ARG90 |
D | PRO179 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 3081 |
Chain | Residue |
A | ARG90 |
A | PRO179 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 3082 |
Chain | Residue |
A | GLY180 |
A | PHE181 |
A | SER182 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 3083 |
Chain | Residue |
D | ARG224 |
D | ARG233 |
D | HOH1050 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 3084 |
Chain | Residue |
F | LYS241 |
F | ARG242 |
F | ARG244 |
F | HOH1175 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 3085 |
Chain | Residue |
B | SER189 |
B | SER192 |
B | ARG242 |
B | ARG244 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 500 |
Chain | Residue |
A | HIS120 |
A | ASP143 |
A | ASP147 |
A | ASP251 |
A | MN501 |
A | S2C551 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 501 |
Chain | Residue |
A | ASP143 |
A | HIS145 |
A | ASP251 |
A | ASP253 |
A | MN500 |
A | S2C551 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 502 |
Chain | Residue |
B | HIS120 |
B | ASP143 |
B | ASP147 |
B | ASP251 |
B | MN503 |
B | S2C552 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 503 |
Chain | Residue |
B | ASP143 |
B | HIS145 |
B | ASP251 |
B | ASP253 |
B | MN502 |
B | S2C552 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 504 |
Chain | Residue |
C | ASP143 |
C | HIS145 |
C | ASP251 |
C | ASP253 |
C | MN505 |
C | S2C553 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 505 |
Chain | Residue |
C | HIS120 |
C | ASP143 |
C | ASP147 |
C | ASP251 |
C | MN504 |
C | S2C553 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 506 |
Chain | Residue |
D | HIS120 |
D | ASP143 |
D | ASP147 |
D | ASP251 |
D | MN507 |
D | S2C554 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 507 |
Chain | Residue |
D | ASP143 |
D | HIS145 |
D | ASP251 |
D | ASP253 |
D | MN506 |
D | S2C554 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 508 |
Chain | Residue |
E | HIS120 |
E | ASP143 |
E | ASP147 |
E | ASP251 |
E | MN509 |
E | S2C555 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 509 |
Chain | Residue |
E | HIS145 |
E | ASP251 |
E | ASP253 |
E | MN508 |
E | S2C555 |
E | ASP143 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 510 |
Chain | Residue |
F | ASP143 |
F | HIS145 |
F | ASP251 |
F | ASP253 |
F | MN511 |
F | S2C556 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 511 |
Chain | Residue |
F | HIS120 |
F | ASP143 |
F | ASP147 |
F | ASP251 |
F | MN510 |
F | S2C556 |
site_id | DC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL E 600 |
Chain | Residue |
E | ARG242 |
site_id | DC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 601 |
Chain | Residue |
C | ARG50 |
C | GLU51 |
C | GLY53 |
C | HOH939 |
site_id | DC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL C 602 |
Chain | Residue |
C | GLN243 |
site_id | DC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL F 605 |
Chain | Residue |
F | GLN243 |
site_id | DC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE S2C A 551 |
Chain | Residue |
A | HIS120 |
A | ASP143 |
A | HIS145 |
A | ASP147 |
A | ASN149 |
A | SER156 |
A | HIS160 |
A | GLY161 |
A | ASP202 |
A | ASP251 |
A | ASP253 |
A | GLU296 |
A | MN500 |
A | MN501 |
A | HOH917 |
A | HOH918 |
A | HOH925 |
A | HOH1076 |
A | HOH1205 |
site_id | DC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE S2C B 552 |
Chain | Residue |
B | HIS120 |
B | ASP143 |
B | HIS145 |
B | ASP147 |
B | ASN149 |
B | SER156 |
B | HIS160 |
B | GLY161 |
B | ASP202 |
B | ASP251 |
B | ASP253 |
B | THR265 |
B | GLU296 |
B | MN502 |
B | MN503 |
B | HOH920 |
B | HOH921 |
B | HOH999 |
site_id | DC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE S2C C 553 |
Chain | Residue |
C | HIS120 |
C | ASP143 |
C | HIS145 |
C | ASP147 |
C | ASN149 |
C | THR154 |
C | SER156 |
C | HIS160 |
C | ASP202 |
C | ASP251 |
C | ASP253 |
C | THR265 |
C | GLU296 |
C | MN504 |
C | MN505 |
C | HOH922 |
C | HOH923 |
C | HOH1077 |
C | HOH1147 |
site_id | DC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE S2C D 554 |
Chain | Residue |
D | HIS120 |
D | ASP143 |
D | HIS145 |
D | ASP147 |
D | ASN149 |
D | SER156 |
D | HIS160 |
D | GLY161 |
D | ASP202 |
D | ASP251 |
D | ASP253 |
D | GLU296 |
D | MN506 |
D | MN507 |
D | HOH924 |
D | HOH926 |
D | HOH927 |
D | HOH1078 |
site_id | DC9 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE S2C E 555 |
Chain | Residue |
E | HIS120 |
E | ASP143 |
E | HIS145 |
E | ASP147 |
E | ASN149 |
E | SER156 |
E | HIS160 |
E | GLY161 |
E | ASP202 |
E | ASP251 |
E | ASP253 |
E | THR265 |
E | GLU296 |
E | MN508 |
E | MN509 |
E | HOH931 |
E | HOH932 |
E | HOH933 |
E | HOH1053 |
E | HOH1056 |
site_id | EC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE S2C F 556 |
Chain | Residue |
F | HIS120 |
F | ASP143 |
F | HIS145 |
F | ASP147 |
F | ASN149 |
F | SER156 |
F | HIS160 |
F | ASP202 |
F | ASP251 |
F | ASP253 |
F | THR265 |
F | GLU296 |
F | MN510 |
F | MN511 |
F | HOH928 |
F | HOH929 |
F | HOH930 |
F | HOH1054 |
F | HOH1148 |
Functional Information from PROSITE/UniProt
site_id | PS01053 |
Number of Residues | 22 |
Details | ARGINASE_1 Arginase family signature. SFDIDafdPtlaPAtgtpvvgG |
Chain | Residue | Details |
A | SER249-GLY270 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 54 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12859189, ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE, ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2, ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU, ECO:0007744|PDB:4IXV |
Chain | Residue | Details |
A | HIS120 | |
B | ASP147 | |
B | SER156 | |
B | ASP202 | |
B | ASP251 | |
B | ASP253 | |
B | GLU296 | |
C | HIS120 | |
C | ASP143 | |
C | HIS145 | |
C | ASP147 | |
C | SER156 | |
C | ASP202 | |
C | ASP251 | |
C | ASP253 | |
C | GLU296 | |
D | HIS120 | |
D | ASP143 | |
D | HIS145 | |
D | ASP147 | |
D | SER156 | |
D | ASP202 | |
D | ASP251 | |
D | ASP253 | |
D | GLU296 | |
E | HIS120 | |
E | ASP143 | |
E | HIS145 | |
E | ASP147 | |
E | SER156 | |
E | ASP202 | |
E | ASP251 | |
E | ASP253 | |
E | GLU296 | |
F | HIS120 | |
F | ASP143 | |
F | HIS145 | |
F | ASP147 | |
F | SER156 | |
F | ASP202 | |
F | ASP251 | |
F | ASP253 | |
F | GLU296 | |
A | ASP143 | |
A | HIS145 | |
A | ASP147 | |
A | SER156 | |
A | ASP202 | |
A | ASP251 | |
A | ASP253 | |
A | GLU296 | |
B | HIS120 | |
B | ASP143 | |
B | HIS145 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P53608 |
Chain | Residue | Details |
A | THR265 | |
B | THR265 | |
C | THR265 | |
D | THR265 | |
E | THR265 | |
F | THR265 |