eF-site ID 1n3i-C PDB Code 1n3i Chain 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 C:  DPDELARRAAQVIADRTGIGEHDVAVVLGSGWLPAVAALG SPTTVLPQAELPGFVPPTAAGHAGELLSVPIGAHRVLVLA GRIHAYEGHDLRYVVHPVRAARAAGAQIMVLTNAAGGLRA DLQVGQPVLISDHLNLTARSPLVGGEFVDLTDAYSPRLRE LARQSDPQLAEGVYAGLPGPHYETPAEIRMLQTLGADLVG MSTVHETIAARAAGAEVLGVSLVTNLAAGITGEPLSHAEV LAAGAASATRMGALLADVIARF Description Functional site 1) chain C residue 35 type sequence G description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 2) chain C residue 36 type sequence S description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 3) chain C residue 68 type sequence H description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 4) chain C residue 88 type sequence R description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 5) chain C residue 90 type sequence H description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 6) chain C residue 119 type sequence N description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 7) chain C residue 120 type sequence A description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 8) chain C residue 208 type sequence S description BINDING SITE FOR RESIDUE PO4 C 303 source : AC3 9) chain C residue 153 type sequence F description BINDING SITE FOR RESIDUE DIH B 402 source : AC5 10) chain C residue 36 type sequence S description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 11) chain C residue 90 type sequence H description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 12) chain C residue 92 type sequence Y description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 13) chain C residue 120 type sequence A description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 14) chain C residue 121 type sequence A description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 15) chain C residue 122 type sequence G description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 16) chain C residue 188 type sequence Y description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 17) chain C residue 189 type sequence E description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 18) chain C residue 205 type sequence V description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 19) chain C residue 206 type sequence G description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 20) chain C residue 207 type sequence M description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 21) chain C residue 230 type sequence T description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 22) chain C residue 231 type sequence N description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 23) chain C residue 243 type sequence H description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 24) chain C residue 246 type sequence V description BINDING SITE FOR RESIDUE DIH C 403 source : AC6 25) chain C residue 108 type ACT_SITE sequence R description Proton donor source Swiss-Prot : SWS_FT_FI4 26) chain C residue 211 type BINDING sequence H description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 27) chain C residue 240 type BINDING sequence P description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 28) chain C residue 248 type BINDING sequence A description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 29) chain C residue 101 type BINDING sequence V description BINDING => ECO:0000269|PubMed:16460002 source Swiss-Prot : SWS_FT_FI5 30) chain C residue 125 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 31) chain C residue 138 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI6 32) chain C residue 139 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI6 33) chain C residue 142 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI6 34) chain C residue 217 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI6 35) chain C residue 101 type catalytic sequence V description 229 source MCSA : MCSA3 36) chain C residue 251 type catalytic sequence A description 229 source MCSA : MCSA3 37) chain C residue 105 type catalytic sequence R description 229 source MCSA : MCSA3 38) chain C residue 108 type catalytic sequence R description 229 source MCSA : MCSA3 39) chain C residue 138 type catalytic sequence D description 229 source MCSA : MCSA3 40) chain C residue 139 type catalytic sequence H description 229 source MCSA : MCSA3 41) chain C residue 142 type catalytic sequence L description 229 source MCSA : MCSA3 42) chain C residue 213 type catalytic sequence T description 229 source MCSA : MCSA3 43) chain C residue 249 type catalytic sequence A description 229 source MCSA : MCSA3 44) chain C residue 250 type catalytic sequence G description 229 source MCSA : MCSA3 45) 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 46) 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 47) 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 48) chain C residue 68 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 49) chain C residue 120 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P45563 source Swiss-Prot : SWS_FT_FI2 50) chain C residue 189 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3 51) chain C residue 231 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11444966 source Swiss-Prot : SWS_FT_FI3

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