eF-site ID 1n3i-A PDB Code 1n3i Chain A click to enlarge Title Crystal Structure of Mycobacterium tuberculosis PNP with transition state analog DADMe-ImmH Classification TRANSFERASE Compound Purine Nucleoside Phosphorylase Source (PUNA_MYCTU) Sequence A:  DPDELARRAAQVIADRTGIGEHDVAVVLGSGWLPAVAALG SPTTVLPQAELPGFVPPTAAGHAGELLSVPIGAHRVLVLA GRIHAYEGHDLRYVVHPVRAARAAGAQIMVLTNAAGGLRA DLQVGQPVLISDHLNLTARSPLVGGEFVDLTDAYSPRLRE LARQSDPQLAEGVYAGLPGPHYETPAEIRMLQTLGADLVG MSTVHETIAARAAGAEVLGVSLVTNLAAGITGEPLSHAEV LAAGAASATRMGALLADVIARF Description Functional site 1) chain A residue 35 type sequence G description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 2) chain A residue 36 type sequence S description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 3) chain A residue 68 type sequence H description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 4) chain A residue 88 type sequence R description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 5) chain A residue 90 type sequence H description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 6) chain A residue 119 type sequence N description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 7) chain A residue 120 type sequence A description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 8) chain A residue 208 type sequence S description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 9) chain A residue 90 type sequence H description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 10) chain A residue 92 type sequence Y description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 11) chain A residue 120 type sequence A description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 12) chain A residue 121 type sequence A description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 13) chain A residue 122 type sequence G description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 14) chain A residue 188 type sequence Y description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 15) chain A residue 189 type sequence E description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 16) chain A residue 205 type sequence V description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 17) chain A residue 206 type sequence G description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 18) chain A residue 207 type sequence M description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 19) chain A residue 230 type sequence T description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 20) chain A residue 231 type sequence N description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 21) chain A residue 243 type sequence H description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 22) chain A residue 246 type sequence V description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 23) chain A residue 108 type ACT_SITE sequence R description Proton donor source Swiss-Prot : SWS_FT_FI4 24) chain A residue 101 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 25) chain A residue 211 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 240 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 248 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 125 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 29) chain A residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI6 30) chain A residue 139 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI6 31) chain A residue 142 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI6 32) chain A residue 217 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 33) chain A residue 101 type catalytic sequence V description 229 source MCSA : MCSA1 34) chain A residue 251 type catalytic sequence A description 229 source MCSA : MCSA1 35) chain A residue 105 type catalytic sequence R description 229 source MCSA : MCSA1 36) chain A residue 108 type catalytic sequence R description 229 source MCSA : MCSA1 37) chain A residue 138 type catalytic sequence D description 229 source MCSA : MCSA1 38) chain A residue 139 type catalytic sequence H description 229 source MCSA : MCSA1 39) chain A residue 142 type catalytic sequence L description 229 source MCSA : MCSA1 40) chain A residue 213 type catalytic sequence T description 229 source MCSA : MCSA1 41) chain A residue 249 type catalytic sequence A description 229 source MCSA : MCSA1 42) chain A residue 250 type catalytic sequence G description 229 source MCSA : MCSA1 43) chain A residue 36 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11444966, ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 88 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11444966, ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 208 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11444966, ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 68 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 120 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 189 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 231 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 83-124 type prosite sequence LVLAGRIHAYEGHDLRYVVHPVRAARAAGAQIMVLTNAAG GL description PNP_MTAP_2 Purine and other phosphorylases family 2 signature. LvlaGriHaYeghdLryvVhpVrAaraaGaqi.MVltNAaGGL source prosite : PS01240

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