1GPM
ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003921 | molecular_function | GMP synthase activity |
| A | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046037 | biological_process | GMP metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003921 | molecular_function | GMP synthase activity |
| B | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006177 | biological_process | GMP biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046037 | biological_process | GMP metabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003921 | molecular_function | GMP synthase activity |
| C | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0006177 | biological_process | GMP biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046037 | biological_process | GMP metabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003921 | molecular_function | GMP synthase activity |
| D | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0006177 | biological_process | GMP biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046037 | biological_process | GMP metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 528 |
| Chain | Residue |
| A | LYS517 |
| A | THR521 |
| A | ILE522 |
| A | GLU523 |
| A | HOH732 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 528 |
| Chain | Residue |
| B | LYS517 |
| B | THR521 |
| B | ILE522 |
| B | GLU523 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 530 |
| Chain | Residue |
| B | POP526 |
| B | AMP527 |
| B | HOH609 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 528 |
| Chain | Residue |
| C | LYS517 |
| C | THR521 |
| C | ILE522 |
| C | GLU523 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 530 |
| Chain | Residue |
| C | POP526 |
| C | AMP527 |
| C | HOH712 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 D 528 |
| Chain | Residue |
| D | LYS517 |
| D | THR521 |
| D | ILE522 |
| D | GLU523 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 530 |
| Chain | Residue |
| D | POP526 |
| D | AMP527 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE POP A 526 |
| Chain | Residue |
| A | SER235 |
| A | GLY237 |
| A | VAL238 |
| A | ASP239 |
| A | SER240 |
| A | LYS381 |
| A | AMP527 |
| A | HOH538 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AMP A 527 |
| Chain | Residue |
| A | GLY233 |
| A | LEU234 |
| A | SER235 |
| A | VAL258 |
| A | VAL260 |
| A | PHE315 |
| A | POP526 |
| A | HOH622 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CIT A 529 |
| Chain | Residue |
| A | SER17 |
| A | GLN18 |
| A | GLY58 |
| A | GLY59 |
| A | PRO60 |
| A | CYS86 |
| A | TYR87 |
| A | SER142 |
| A | HIS181 |
| A | HOH653 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POP B 526 |
| Chain | Residue |
| B | SER235 |
| B | GLY237 |
| B | VAL238 |
| B | ASP239 |
| B | SER240 |
| B | LYS381 |
| B | AMP527 |
| B | MG530 |
| B | HOH557 |
| B | HOH609 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP B 527 |
| Chain | Residue |
| B | GLY233 |
| B | LEU234 |
| B | SER235 |
| B | SER240 |
| B | VAL258 |
| B | VAL260 |
| B | PHE315 |
| B | POP526 |
| B | MG530 |
| B | HOH609 |
| B | HOH635 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CIT B 529 |
| Chain | Residue |
| B | SER17 |
| B | GLN18 |
| B | GLY58 |
| B | GLY59 |
| B | PRO60 |
| B | CYS86 |
| B | TYR87 |
| B | SER142 |
| B | HIS181 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE POP C 526 |
| Chain | Residue |
| C | AMP527 |
| C | MG530 |
| C | HOH712 |
| C | SER235 |
| C | GLY237 |
| C | VAL238 |
| C | ASP239 |
| C | SER240 |
| C | LYS381 |
| site_id | BC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP C 527 |
| Chain | Residue |
| C | GLY233 |
| C | LEU234 |
| C | SER235 |
| C | SER240 |
| C | VAL258 |
| C | VAL260 |
| C | PHE315 |
| C | POP526 |
| C | MG530 |
| C | HOH569 |
| C | HOH637 |
| C | HOH660 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CIT C 529 |
| Chain | Residue |
| C | SER17 |
| C | GLN18 |
| C | GLY58 |
| C | GLY59 |
| C | PRO60 |
| C | CYS86 |
| C | TYR87 |
| C | SER142 |
| C | HIS181 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POP D 526 |
| Chain | Residue |
| D | SER235 |
| D | GLY237 |
| D | VAL238 |
| D | ASP239 |
| D | SER240 |
| D | LYS381 |
| D | AMP527 |
| D | MG530 |
| D | HOH646 |
| D | HOH668 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AMP D 527 |
| Chain | Residue |
| D | GLY233 |
| D | LEU234 |
| D | SER235 |
| D | VAL258 |
| D | VAL260 |
| D | PHE315 |
| D | GLY405 |
| D | POP526 |
| D | MG530 |
| D | HOH667 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CIT D 529 |
| Chain | Residue |
| D | SER17 |
| D | GLN18 |
| D | GLY58 |
| D | GLY59 |
| D | PRO60 |
| D | CYS86 |
| D | TYR87 |
| D | PHE108 |
| D | SER142 |
| D | HIS181 |
| site_id | GAA |
| Number of Residues | 3 |
| Details | G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES |
| Chain | Residue |
| A | CYS86 |
| A | HIS181 |
| A | GLU183 |
| site_id | GBA |
| Number of Residues | 3 |
| Details | G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES |
| Chain | Residue |
| B | CYS86 |
| B | HIS181 |
| B | GLU183 |
| site_id | GCA |
| Number of Residues | 3 |
| Details | G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES |
| Chain | Residue |
| C | CYS86 |
| C | HIS181 |
| C | GLU183 |
| site_id | GDA |
| Number of Residues | 3 |
| Details | G-TYPE GLUTAMINE AMIDOTRANSFERASE ACTIVE SITE. THESE RESIDUES ARE ARRANGED IN A CATALYTIC TRIAD SIMILAR TO THOSE FOUND IN OTHER HYDROLYTIC ENZYMES |
| Chain | Residue |
| D | CYS86 |
| D | HIS181 |
| D | GLU183 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | CYS86 | |
| B | CYS86 | |
| C | CYS86 | |
| D | CYS86 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | HIS181 | |
| A | GLU183 | |
| B | HIS181 | |
| B | GLU183 | |
| C | HIS181 | |
| C | GLU183 | |
| D | HIS181 | |
| D | GLU183 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER235 | |
| B | SER235 | |
| C | SER235 | |
| D | SER235 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 234 |
| Chain | Residue | Details |
| A | GLY59 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS86 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | TYR87 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS181 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU183 | hydrogen bond acceptor, increase acidity, increase basicity |
| A | ASP239 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role |
| A | LYS381 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 234 |
| Chain | Residue | Details |
| B | GLY59 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS86 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | TYR87 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS181 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU183 | hydrogen bond acceptor, increase acidity, increase basicity |
| B | ASP239 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role |
| B | LYS381 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 234 |
| Chain | Residue | Details |
| C | GLY59 | electrostatic stabiliser, hydrogen bond donor |
| C | CYS86 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | TYR87 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS181 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLU183 | hydrogen bond acceptor, increase acidity, increase basicity |
| C | ASP239 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role |
| C | LYS381 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 234 |
| Chain | Residue | Details |
| D | GLY59 | electrostatic stabiliser, hydrogen bond donor |
| D | CYS86 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | TYR87 | electrostatic stabiliser, hydrogen bond donor |
| D | HIS181 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLU183 | hydrogen bond acceptor, increase acidity, increase basicity |
| D | ASP239 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, steric role |
| D | LYS381 | electrostatic stabiliser, hydrogen bond donor |
