1N3I
Crystal Structure of Mycobacterium tuberculosis PNP with transition state analog DADMe-ImmH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0016763 | molecular_function | pentosyltransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
B | 0009116 | biological_process | nucleoside metabolic process |
B | 0016763 | molecular_function | pentosyltransferase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
C | 0009116 | biological_process | nucleoside metabolic process |
C | 0016763 | molecular_function | pentosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 301 |
Chain | Residue |
A | GLY35 |
A | HOH561 |
A | SER36 |
A | HIS68 |
A | ARG88 |
A | HIS90 |
A | ASN119 |
A | ALA120 |
A | SER208 |
A | DIH401 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 B 302 |
Chain | Residue |
B | GLY35 |
B | SER36 |
B | HIS68 |
B | ARG88 |
B | HIS90 |
B | ASN119 |
B | ALA120 |
B | SER208 |
B | DIH402 |
B | HOH532 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 C 303 |
Chain | Residue |
C | GLY35 |
C | SER36 |
C | HIS68 |
C | ARG88 |
C | HIS90 |
C | ASN119 |
C | ALA120 |
C | SER208 |
C | DIH403 |
C | HOH610 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE DIH A 401 |
Chain | Residue |
A | HIS90 |
A | TYR92 |
A | ALA120 |
A | ALA121 |
A | GLY122 |
A | TYR188 |
A | GLU189 |
A | VAL205 |
A | GLY206 |
A | MET207 |
A | THR230 |
A | ASN231 |
A | HIS243 |
A | VAL246 |
A | PO4301 |
A | HOH601 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE DIH B 402 |
Chain | Residue |
B | HIS90 |
B | TYR92 |
B | ALA120 |
B | ALA121 |
B | GLY122 |
B | TYR188 |
B | GLU189 |
B | VAL205 |
B | GLY206 |
B | MET207 |
B | THR230 |
B | ASN231 |
B | HIS243 |
B | VAL246 |
B | PO4302 |
B | HOH621 |
C | PHE153 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE DIH C 403 |
Chain | Residue |
C | SER36 |
C | HIS90 |
C | TYR92 |
C | ALA120 |
C | ALA121 |
C | GLY122 |
C | TYR188 |
C | GLU189 |
C | VAL205 |
C | GLY206 |
C | MET207 |
C | THR230 |
C | ASN231 |
C | HIS243 |
C | VAL246 |
C | PO4303 |
C | HOH520 |
Functional Information from PROSITE/UniProt
site_id | PS01240 |
Number of Residues | 42 |
Details | PNP_MTAP_2 Purine and other phosphorylases family 2 signature. LvlaGriHaYeghdLryvVhpVrAaraaGaqi.MVltNAaGGL |
Chain | Residue | Details |
A | LEU83-LEU124 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11444966, ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80 |
Chain | Residue | Details |
A | SER36 | |
A | ARG88 | |
A | SER208 | |
B | SER36 | |
B | ARG88 | |
B | SER208 | |
C | SER36 | |
C | ARG88 | |
C | SER208 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P45563 |
Chain | Residue | Details |
A | HIS68 | |
A | ALA120 | |
B | HIS68 | |
B | ALA120 | |
C | HIS68 | |
C | ALA120 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11444966 |
Chain | Residue | Details |
A | GLU189 | |
A | ASN231 | |
B | GLU189 | |
B | ASN231 | |
C | GLU189 | |
C | ASN231 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | ARG108 | |
B | ARG108 | |
C | ARG108 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16460002 |
Chain | Residue | Details |
A | VAL101 | |
C | HIS211 | |
C | PRO240 | |
C | ALA248 | |
A | HIS211 | |
A | PRO240 | |
A | ALA248 | |
B | VAL101 | |
B | HIS211 | |
B | PRO240 | |
B | ALA248 | |
C | VAL101 |
site_id | SWS_FT_FI6 |
Number of Residues | 15 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG125 | |
B | ARG217 | |
C | ARG125 | |
C | ASP138 | |
C | HIS139 | |
C | LEU142 | |
C | ARG217 | |
A | ASP138 | |
A | HIS139 | |
A | LEU142 | |
A | ARG217 | |
B | ARG125 | |
B | ASP138 | |
B | HIS139 | |
B | LEU142 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ula |
Chain | Residue | Details |
A | HIS90 | |
A | ASN231 | |
A | GLU93 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ula |
Chain | Residue | Details |
B | HIS90 | |
B | ASN231 | |
B | GLU93 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ula |
Chain | Residue | Details |
C | HIS90 | |
C | ASN231 | |
C | GLU93 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 229 |
Chain | Residue | Details |
A | VAL101 | electrostatic stabiliser |
A | ALA251 | electrostatic stabiliser, hydrogen bond donor |
A | ARG105 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
A | ARG108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
A | ASP138 | metal ligand |
A | HIS139 | metal ligand |
A | LEU142 | metal ligand |
A | THR213 | electrostatic stabiliser |
A | ALA249 | electrostatic stabiliser, hydrogen bond donor |
A | GLY250 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 229 |
Chain | Residue | Details |
B | VAL101 | electrostatic stabiliser |
B | ALA251 | electrostatic stabiliser, hydrogen bond donor |
B | ARG105 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
B | ARG108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
B | ASP138 | metal ligand |
B | HIS139 | metal ligand |
B | LEU142 | metal ligand |
B | THR213 | electrostatic stabiliser |
B | ALA249 | electrostatic stabiliser, hydrogen bond donor |
B | GLY250 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 10 |
Details | M-CSA 229 |
Chain | Residue | Details |
C | VAL101 | electrostatic stabiliser |
C | ALA251 | electrostatic stabiliser, hydrogen bond donor |
C | ARG105 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
C | ARG108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
C | ASP138 | metal ligand |
C | HIS139 | metal ligand |
C | LEU142 | metal ligand |
C | THR213 | electrostatic stabiliser |
C | ALA249 | electrostatic stabiliser, hydrogen bond donor |
C | GLY250 | electrostatic stabiliser, hydrogen bond donor |