eF-site ID 1n3i-ABC PDB Code 1n3i Chain A, B, C 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 B:  DPDELARRAAQVIADRTGIGEHDVAVVLGSGWLPAVAALG SPTTVLPQAELPGFVPPTAAGHAGELLSVPIGAHRVLVLA GRIHAYEGHDLRYVVHPVRAARAAGAQIMVLTNAAGGLRA DLQVGQPVLISDHLNLTARSPLVGGEFVDLTDAYSPRLRE LARQSDPQLAEGVYAGLPGPHYETPAEIRMLQTLGADLVG MSTVHETIAARAAGAEVLGVSLVTNLAAGITGEPLSHAEV LAAGAASATRMGALLADVIARF C:  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 B residue 35 type sequence G description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 10) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 11) chain B residue 68 type sequence H description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 12) chain B residue 88 type sequence R description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 13) chain B residue 90 type sequence H description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 14) chain B residue 119 type sequence N description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 15) chain B residue 120 type sequence A description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 16) chain B residue 208 type sequence S description BINDING SITE FOR RESIDUE PO4 B 302 source : AC2 17) chain C residue 35 type sequence G description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 18) chain C residue 36 type sequence S description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 19) chain C residue 68 type sequence H description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 20) chain C residue 88 type sequence R description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 21) chain C residue 90 type sequence H description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 22) chain C residue 119 type sequence N description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 23) chain C residue 120 type sequence A description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 24) chain C residue 208 type sequence S description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 25) chain A residue 90 type sequence H description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 26) chain A residue 92 type sequence Y description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 27) chain A residue 120 type sequence A description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 28) chain A residue 121 type sequence A description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 29) chain A residue 122 type sequence G description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 30) chain A residue 188 type sequence Y description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 31) chain A residue 189 type sequence E description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 32) chain A residue 205 type sequence V description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 33) chain A residue 206 type sequence G description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 34) chain A residue 207 type sequence M description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 35) chain A residue 230 type sequence T description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 36) chain A residue 231 type sequence N description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 37) chain A residue 243 type sequence H description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 38) chain A residue 246 type sequence V description BINDING SITE FOR RESIDUE DIH A 401 source : AC4 39) chain B residue 90 type sequence H description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 40) chain B residue 92 type sequence Y description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 41) chain B residue 120 type sequence A description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 42) chain B residue 121 type sequence A description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 43) chain B residue 122 type sequence G description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 44) chain B residue 188 type sequence Y description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 45) chain B residue 189 type sequence E description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 46) chain B residue 205 type sequence V description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 47) chain B residue 206 type sequence G description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 48) chain B residue 207 type sequence M description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 49) chain B residue 230 type sequence T description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 50) chain B residue 231 type sequence N description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 51) chain B residue 243 type sequence H description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 52) chain B residue 246 type sequence V description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 53) chain C residue 153 type sequence F description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 54) chain C residue 36 type sequence S description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 55) chain C residue 90 type sequence H description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 56) chain C residue 92 type sequence Y description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 57) chain C residue 120 type sequence A description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 58) chain C residue 121 type sequence A description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 59) chain C residue 122 type sequence G description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 60) chain C residue 188 type sequence Y description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 61) chain C residue 189 type sequence E description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 62) chain C residue 205 type sequence V description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 63) chain C residue 206 type sequence G description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 64) chain C residue 207 type sequence M description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 65) chain C residue 230 type sequence T description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 66) chain C residue 231 type sequence N description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 67) chain C residue 243 type sequence H description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 68) chain C residue 246 type sequence V description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 69) chain A residue 108 type ACT_SITE sequence R description Proton donor source Swiss-Prot : SWS_FT_FI4 70) chain B residue 108 type ACT_SITE sequence R description Proton donor source Swiss-Prot : SWS_FT_FI4 71) chain C residue 108 type ACT_SITE sequence R description Proton donor source Swiss-Prot : SWS_FT_FI4 72) chain A residue 101 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 73) chain C residue 211 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 74) chain C residue 240 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 75) chain C residue 248 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 76) chain A residue 211 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 77) chain A residue 240 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 78) chain A residue 248 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 79) chain B residue 101 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 80) chain B residue 211 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 81) chain B residue 240 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 82) chain B residue 248 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 83) chain C residue 101 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 84) chain A residue 125 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 85) chain B residue 217 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 86) chain C residue 125 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 87) chain C residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI6 88) chain C residue 139 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI6 89) chain C residue 142 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI6 90) chain C residue 217 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 91) chain A residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI6 92) chain A residue 139 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI6 93) chain A residue 142 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI6 94) chain A residue 217 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 95) chain B residue 125 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 96) chain B residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI6 97) chain B residue 139 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI6 98) chain B residue 142 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI6 99) chain A residue 101 type catalytic sequence V description 229 source MCSA : MCSA1 100) chain A residue 251 type catalytic sequence A description 229 source MCSA : MCSA1 101) chain A residue 105 type catalytic sequence R description 229 source MCSA : MCSA1 102) chain A residue 108 type catalytic sequence R description 229 source MCSA : MCSA1 103) chain A residue 138 type catalytic sequence D description 229 source MCSA : MCSA1 104) chain A residue 139 type catalytic sequence H description 229 source MCSA : MCSA1 105) chain A residue 142 type catalytic sequence L description 229 source MCSA : MCSA1 106) chain A residue 213 type catalytic sequence T description 229 source MCSA : MCSA1 107) chain A residue 249 type catalytic sequence A description 229 source MCSA : MCSA1 108) chain A residue 250 type catalytic sequence G description 229 source MCSA : MCSA1 109) chain B residue 101 type catalytic sequence V description 229 source MCSA : MCSA2 110) chain B residue 251 type catalytic sequence A description 229 source MCSA : MCSA2 111) chain B residue 105 type catalytic sequence R description 229 source MCSA : MCSA2 112) chain B residue 108 type catalytic sequence R description 229 source MCSA : MCSA2 113) chain B residue 138 type catalytic sequence D description 229 source MCSA : MCSA2 114) chain B residue 139 type catalytic sequence H description 229 source MCSA : MCSA2 115) chain B residue 142 type catalytic sequence L description 229 source MCSA : MCSA2 116) chain B residue 213 type catalytic sequence T description 229 source MCSA : MCSA2 117) chain B residue 249 type catalytic sequence A description 229 source MCSA : MCSA2 118) chain B residue 250 type catalytic sequence G description 229 source MCSA : MCSA2 119) chain C residue 101 type catalytic sequence V description 229 source MCSA : MCSA3 120) chain C residue 251 type catalytic sequence A description 229 source MCSA : MCSA3 121) chain C residue 105 type catalytic sequence R description 229 source MCSA : MCSA3 122) chain C residue 108 type catalytic sequence R description 229 source MCSA : MCSA3 123) chain C residue 138 type catalytic sequence D description 229 source MCSA : MCSA3 124) chain C residue 139 type catalytic sequence H description 229 source MCSA : MCSA3 125) chain C residue 142 type catalytic sequence L description 229 source MCSA : MCSA3 126) chain C residue 213 type catalytic sequence T description 229 source MCSA : MCSA3 127) chain C residue 249 type catalytic sequence A description 229 source MCSA : MCSA3 128) chain C residue 250 type catalytic sequence G description 229 source MCSA : MCSA3 129) 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 130) 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 131) 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 132) chain B 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 133) chain B 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 134) chain B 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 135) chain C 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 136) chain C 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 137) chain C 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 138) chain A residue 68 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 139) chain A residue 120 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 140) chain B residue 68 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 141) chain B residue 120 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 142) chain C residue 68 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 143) chain C residue 120 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 144) chain A residue 189 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 145) chain A residue 231 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 146) chain B residue 189 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 147) chain B residue 231 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 148) chain C residue 189 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 149) chain C residue 231 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 150) 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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