3VPB
ArgX from Sulfolobus tokodaii complexed with LysW/Glu/ADP/Mg/Zn/Sulfate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006526 | biological_process | L-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 | 0043774 | molecular_function | coenzyme F420-2 alpha-glutamyl ligase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006526 | biological_process | L-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 | 0043774 | molecular_function | coenzyme F420-2 alpha-glutamyl ligase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006526 | biological_process | L-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 | 0043774 | molecular_function | coenzyme F420-2 alpha-glutamyl ligase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006526 | biological_process | L-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 | 0043774 | molecular_function | coenzyme F420-2 alpha-glutamyl ligase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0006526 | biological_process | L-arginine biosynthetic process |
E | 0009085 | biological_process | lysine biosynthetic process |
E | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
E | 0046872 | molecular_function | metal ion binding |
F | 0006526 | biological_process | L-arginine biosynthetic process |
F | 0009085 | biological_process | lysine biosynthetic process |
F | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
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 | ASP237 |
A | LEU239 |
A | ASN249 |
A | GLU250 |
A | LYS127 |
A | MG502 |
A | ZN503 |
A | SO4504 |
A | HOH621 |
A | HOH624 |
A | HOH642 |
A | HOH696 |
A | GLY131 |
A | SER132 |
A | TRP133 |
A | GLY134 |
A | VAL137 |
A | GLN167 |
A | GLU168 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GLU A 501 |
Chain | Residue |
A | TYR190 |
A | ARG192 |
A | ASN202 |
A | VAL203 |
A | ALA204 |
A | GLU256 |
A | LYS258 |
A | GLY259 |
A | PHE260 |
A | SO4504 |
A | HOH626 |
A | HOH635 |
E | GLU56 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | ASP237 |
A | GLU250 |
A | ADP500 |
A | ZN503 |
A | SO4504 |
A | HOH642 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 503 |
Chain | Residue |
A | GLU250 |
A | ASN252 |
A | ADP500 |
A | MG502 |
A | SO4504 |
A | HOH696 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | SER132 |
A | TRP133 |
A | ARG178 |
A | ARG192 |
A | ASN202 |
A | ASP237 |
A | GLU250 |
A | ASN252 |
A | ADP500 |
A | GLU501 |
A | MG502 |
A | ZN503 |
A | HOH642 |
E | GLU56 |
site_id | AC6 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE ADP B 500 |
Chain | Residue |
B | LYS87 |
B | LYS127 |
B | GLY131 |
B | SER132 |
B | TRP133 |
B | GLY134 |
B | GLN167 |
B | GLU168 |
B | TYR169 |
B | ILE170 |
B | ASP176 |
B | ARG200 |
B | ALA201 |
B | ASN202 |
B | ASP237 |
B | ASN249 |
B | GLU250 |
B | MG502 |
B | ZN503 |
B | SO4504 |
B | HOH617 |
B | HOH621 |
B | HOH650 |
B | HOH651 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GLU B 501 |
Chain | Residue |
B | SO4504 |
B | HOH654 |
B | HOH658 |
B | HOH689 |
F | GLU56 |
B | ARG178 |
B | TYR190 |
B | ARG192 |
B | ASN202 |
B | VAL203 |
B | ALA204 |
B | GLU256 |
B | LYS258 |
B | GLY259 |
B | PHE260 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | ASP237 |
B | GLU250 |
B | ADP500 |
B | ZN503 |
B | SO4504 |
B | HOH650 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 503 |
Chain | Residue |
B | GLU250 |
B | ASN252 |
B | ADP500 |
B | MG502 |
B | SO4504 |
B | HOH651 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SO4 B 504 |
Chain | Residue |
B | SER132 |
B | TRP133 |
B | ARG178 |
B | ARG192 |
B | ASN202 |
B | ASP237 |
B | GLU250 |
B | ASN252 |
B | ADP500 |
B | GLU501 |
B | MG502 |
B | ZN503 |
B | HOH650 |
F | GLU56 |
site_id | BC2 |
Number of Residues | 27 |
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 | ASN202 |
C | ASP237 |
C | ASN249 |
C | GLU250 |
C | MG502 |
C | SO4503 |
C | HOH633 |
C | HOH651 |
C | HOH706 |
C | HOH709 |
C | HOH731 |
site_id | BC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLU C 501 |
Chain | Residue |
C | TRP133 |
C | TYR190 |
C | ARG192 |
C | ASN202 |
C | VAL203 |
C | ALA204 |
C | GLU256 |
C | LYS258 |
C | GLY259 |
C | PHE260 |
C | SO4503 |
C | HOH639 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 502 |
Chain | Residue |
C | ASP237 |
C | GLU250 |
C | ADP500 |
C | SO4503 |
C | HOH709 |
site_id | BC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SO4 C 503 |
Chain | Residue |
C | SER132 |
C | TRP133 |
C | ARG178 |
C | ARG192 |
C | ASN202 |
C | ASP237 |
C | GLU250 |
C | ASN252 |
C | ADP500 |
C | GLU501 |
C | MG502 |
C | HOH601 |
C | HOH633 |
C | HOH709 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 504 |
Chain | Residue |
C | SER56 |
C | MET57 |
C | TYR58 |
D | SER159 |
site_id | BC7 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE ADP D 500 |
Chain | Residue |
D | LYS87 |
D | ILE125 |
D | LYS127 |
D | GLY131 |
D | SER132 |
D | TRP133 |
D | GLY134 |
D | VAL137 |
D | GLN167 |
D | GLU168 |
D | TYR169 |
D | ILE170 |
D | ASP176 |
D | ARG200 |
D | ALA201 |
D | ASN202 |
D | ASP237 |
D | ASN249 |
D | GLU250 |
D | MG502 |
D | SO4503 |
D | HOH648 |
D | HOH654 |
D | HOH690 |
D | HOH699 |
site_id | BC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GLU D 501 |
Chain | Residue |
D | TRP133 |
D | TYR190 |
D | ARG192 |
D | ASN202 |
D | VAL203 |
D | ALA204 |
D | GLU256 |
D | LYS258 |
D | GLY259 |
D | PHE260 |
D | SO4503 |
D | HOH627 |
D | HOH680 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 502 |
Chain | Residue |
D | ASP237 |
D | GLU250 |
D | ADP500 |
D | SO4503 |
D | HOH690 |
site_id | CC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SO4 D 503 |
Chain | Residue |
D | SER132 |
D | TRP133 |
D | ARG178 |
D | ARG192 |
D | ASN202 |
D | ASP237 |
D | GLU250 |
D | ASN252 |
D | ADP500 |
D | GLU501 |
D | MG502 |
D | HOH608 |
D | HOH654 |
D | HOH690 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 504 |
Chain | Residue |
C | SER159 |
D | SER56 |
D | MET57 |
D | TYR58 |
D | HOH803 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 100 |
Chain | Residue |
E | CYS6 |
E | CYS9 |
E | HIS27 |
E | CYS29 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 100 |
Chain | Residue |
F | CYS6 |
F | CYS9 |
F | HIS27 |
F | CYS29 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 66 |
Details | ZN_FING: TFIIB-type |
Chain | Residue | Details |
E | MET1-GLU34 | |
B | LYS127 | |
B | GLY131 | |
B | GLN167 | |
B | ARG192 | |
B | ASN202 | |
B | VAL203 | |
B | GLU256 | |
C | LYS87 | |
C | LYS127 | |
C | GLY131 | |
F | MET1-GLU34 | |
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 | 8 |
Details | BINDING: |
Chain | Residue | Details |
E | CYS6 | |
D | ASP237 | |
D | GLU250 | |
D | ASN252 | |
E | CYS9 | |
E | HIS27 | |
E | CYS29 | |
F | CYS6 | |
F | CYS9 | |
F | HIS27 | |
F | CYS29 | |
C | ASN252 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: 5-glutamyl N2-ornithine; alternate => ECO:0000305 |
Chain | Residue | Details |
E | GLU56 | |
F | GLU56 |