3VPC
ArgX from Sulfolobus tokodaii complexed with ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006526 | biological_process | arginine biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0036211 | biological_process | protein modification process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006526 | biological_process | arginine biosynthetic process |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0036211 | biological_process | protein modification process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006526 | biological_process | arginine biosynthetic process |
| C | 0009085 | biological_process | lysine biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0036211 | biological_process | protein modification process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006526 | biological_process | arginine biosynthetic process |
| D | 0009085 | biological_process | lysine biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0036211 | biological_process | protein modification process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP A 500 |
| Chain | Residue |
| A | LYS87 |
| A | TYR169 |
| A | ILE170 |
| A | ASP176 |
| A | ARG200 |
| A | ALA201 |
| A | ASN202 |
| A | ASN249 |
| A | GLU250 |
| A | HOH601 |
| A | HOH624 |
| A | ILE125 |
| A | HOH714 |
| A | HOH756 |
| A | HOH823 |
| A | LYS127 |
| A | SER132 |
| A | TRP133 |
| A | GLY134 |
| A | VAL137 |
| A | GLN167 |
| A | GLU168 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP B 500 |
| Chain | Residue |
| B | LYS87 |
| B | ILE125 |
| B | LYS127 |
| B | SER132 |
| B | TRP133 |
| B | GLY134 |
| B | VAL137 |
| B | GLN167 |
| B | GLU168 |
| B | TYR169 |
| B | ILE170 |
| B | ASP176 |
| B | ARG200 |
| B | ALA201 |
| B | ASN202 |
| B | ASN249 |
| B | GLU250 |
| B | HOH620 |
| B | HOH706 |
| B | HOH725 |
| B | HOH796 |
| B | HOH810 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP C 500 |
| Chain | Residue |
| C | LYS87 |
| C | ILE125 |
| C | LYS127 |
| C | GLY131 |
| C | SER132 |
| C | TRP133 |
| C | GLY134 |
| C | ARG135 |
| C | VAL137 |
| C | GLN167 |
| C | GLU168 |
| C | TYR169 |
| C | ILE170 |
| C | ASP176 |
| C | ARG200 |
| C | ALA201 |
| C | ASN249 |
| C | GLU250 |
| C | HOH638 |
| C | HOH659 |
| C | HOH664 |
| C | HOH705 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP D 500 |
| Chain | Residue |
| D | LYS87 |
| D | ILE125 |
| D | LYS127 |
| D | SER132 |
| D | TRP133 |
| D | GLY134 |
| D | VAL137 |
| D | GLN167 |
| D | GLU168 |
| D | ILE170 |
| D | ASP176 |
| D | ARG200 |
| D | ALA201 |
| D | ASN202 |
| D | ASN249 |
| D | GLU250 |
| D | HOH618 |
| D | HOH667 |
| D | HOH714 |
| D | HOH760 |
| D | HOH810 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:23434852 |
| Chain | Residue | Details |
| A | LYS87 | |
| B | LYS127 | |
| B | GLY131 | |
| B | GLN167 | |
| B | ARG192 | |
| B | ASN202 | |
| B | VAL203 | |
| B | GLU256 | |
| C | LYS87 | |
| C | LYS127 | |
| C | GLY131 | |
| A | LYS127 | |
| C | GLN167 | |
| C | ARG192 | |
| C | ASN202 | |
| C | VAL203 | |
| C | GLU256 | |
| D | LYS87 | |
| D | LYS127 | |
| D | GLY131 | |
| D | GLN167 | |
| D | ARG192 | |
| A | GLY131 | |
| D | ASN202 | |
| D | VAL203 | |
| D | GLU256 | |
| A | GLN167 | |
| A | ARG192 | |
| A | ASN202 | |
| A | VAL203 | |
| A | GLU256 | |
| B | LYS87 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23434852 |
| Chain | Residue | Details |
| A | ASP237 | |
| D | ASP237 | |
| D | GLU250 | |
| D | ASN252 | |
| A | GLU250 | |
| A | ASN252 | |
| B | ASP237 | |
| B | GLU250 | |
| B | ASN252 | |
| C | ASP237 | |
| C | GLU250 | |
| C | ASN252 |
