1ECC
ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH MN-CPRPP AND 5-OXO-NORLEUCINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0009113 | biological_process | purine nucleobase biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004044 | molecular_function | amidophosphoribosyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0009113 | biological_process | purine nucleobase biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 506 |
| Chain | Residue |
| A | HOH2378 |
| A | HOH2379 |
| A | ASP366 |
| A | ASP367 |
| A | PCP505 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 506 |
| Chain | Residue |
| B | ASP366 |
| B | ASP367 |
| B | PCP505 |
| B | HOH2451 |
| B | HOH2452 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 1449 |
| Chain | Residue |
| A | ASP476 |
| A | THR480 |
| B | GLU376 |
| B | ILE428 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MN A 2376 |
| Chain | Residue |
| A | GLU449 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 2449 |
| Chain | Residue |
| B | GLU449 |
| B | ASP471 |
| B | HOH2543 |
| B | HOH2597 |
| B | HOH2598 |
| B | HOH2599 |
| B | HOH2600 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ONL A 2377 |
| Chain | Residue |
| A | CYS1 |
| A | ARG73 |
| A | TYR74 |
| A | THR76 |
| A | ALA77 |
| A | GLN86 |
| A | ASN101 |
| A | GLY102 |
| A | ASP127 |
| A | SER128 |
| A | HOH2402 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PCP A 505 |
| Chain | Residue |
| A | TYR258 |
| A | GLU303 |
| A | THR304 |
| A | ARG332 |
| A | THR333 |
| A | PHE334 |
| A | LYS349 |
| A | ASP366 |
| A | ASP367 |
| A | SER368 |
| A | ILE369 |
| A | VAL370 |
| A | ARG371 |
| A | GLY372 |
| A | THR373 |
| A | THR374 |
| A | MN506 |
| A | HOH2378 |
| A | HOH2379 |
| A | HOH2411 |
| A | HOH2431 |
| B | ARG328 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ONL B 2450 |
| Chain | Residue |
| B | CYS1 |
| B | ARG73 |
| B | TYR74 |
| B | THR76 |
| B | ALA77 |
| B | GLN86 |
| B | HIS100 |
| B | ASN101 |
| B | GLY102 |
| B | ASP127 |
| B | SER128 |
| B | HOH2482 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE PCP B 505 |
| Chain | Residue |
| A | ARG328 |
| B | TYR258 |
| B | GLU303 |
| B | THR304 |
| B | ARG332 |
| B | THR333 |
| B | PHE334 |
| B | LYS349 |
| B | ASP366 |
| B | ASP367 |
| B | SER368 |
| B | VAL370 |
| B | ARG371 |
| B | GLY372 |
| B | THR373 |
| B | THR374 |
| B | MN506 |
| B | HOH2457 |
| B | HOH2460 |
| B | HOH2502 |
| B | HOH2574 |
| site_id | NTA |
| Number of Residues | 1 |
| Details | NTN AMIDOTRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS THE PRODUCT OF COVALENT INACTIVATION BY THE GLUTAMINE ANALOGUE DON. |
| Chain | Residue |
| A | CYS1 |
| site_id | NTB |
| Number of Residues | 1 |
| Details | NTN AMIDOTRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS THE PRODUCT OF COVALENT INACTIVATION BY THE GLUTAMINE ANALOGUE DON. |
| Chain | Residue |
| B | CYS1 |
| site_id | PRB |
| Number of Residues | 2 |
| Details | PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS CPRPP, A CARBOCYCLIC PRPP ANALOGUE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS, AND ARE THE HALLMARK OF PRTASE ENZYMES. MG++ IS THE PRIMARY BIOLOGICALLY FUNCTIONAL METAL ION. MN++ IS PRESENT IN THIS STRUCTURE, AND DEMONSTRATES A COORDINATION GEOMETRY VERY SIMILAR TO TYPICAL MG++ COORDINATIONS. |
| Chain | Residue |
| B | ASP366 |
| B | ASP367 |
| site_id | PRT |
| Number of Residues | 2 |
| Details | PHOSPHORIBOSYL TRANSFERASE ACTIVE SITE. THE ACTIVE SITE IN THIS STRUCTURE CONTAINS CPRPP, A CARBOCYCLIC PRPP ANALOGUE. ASP 366 AND ASP 367 FUNCTION AS METAL LIGANDS, AND ARE THE HALLMARK OF PRTASE ENZYMES. MG++ IS THE PRIMARY BIOLOGICALLY FUNCTIONAL METAL ION. MN++ IS PRESENT IN THIS STRUCTURE, AND DEMONSTRATES A COORDINATION GEOMETRY VERY SIMILAR TO TYPICAL MG++ COORDINATIONS. |
| Chain | Residue |
| A | ASP366 |
| A | ASP367 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLLVDDSIVRGtT |
| Chain | Residue | Details |
| A | VAL362-THR374 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:7037784 |
| Chain | Residue | Details |
| A | GLY2 | |
| B | GLY2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01931 |
| Chain | Residue | Details |
| A | SER305 | |
| A | ASP367 | |
| A | SER368 | |
| B | SER305 | |
| B | ASP367 | |
| B | SER368 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ecf |
| Chain | Residue | Details |
| A | GLY102 | |
| A | CYS1 | |
| A | ASN101 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ecf |
| Chain | Residue | Details |
| B | GLY102 | |
| B | CYS1 | |
| B | ASN101 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| A | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY27 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | ASN101 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR258 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 214 |
| Chain | Residue | Details |
| B | CYS1 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLY27 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| B | ASN101 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY102 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR258 | electrostatic stabiliser, hydrogen bond donor |
