eF-site ID 1k2y-X PDB Code 1k2y Chain X click to enlarge Title Crystal Structure of Phosphomannomutase/Phosphoglucomutase S108A mutant from P. aeruginosa Classification ISOMERASE Compound phosphomannomutase Source null (ALGC_PSEAE) Sequence X:  KAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESL ARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGM VPTPVLYYAANVLEGKSGVMLTGAHNPPDYNGFKIVVAGE TLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIR DDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYC EVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGD GDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDV KCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAG EMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVF SAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNIT TLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERI KTVFRNQLKAVDSSLPVPF Description Functional site 1) chain X residue 242 type sequence D description BINDING SITE FOR RESIDUE ZN X 500 source : AC1 2) chain X residue 244 type sequence D description BINDING SITE FOR RESIDUE ZN X 500 source : AC1 3) chain X residue 246 type sequence D description BINDING SITE FOR RESIDUE ZN X 500 source : AC1 4) chain X residue 108 type sequence A description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 5) chain X residue 109 type sequence H description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 6) chain X residue 118 type sequence K description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 7) chain X residue 242 type sequence D description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 8) chain X residue 244 type sequence D description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 9) chain X residue 246 type sequence D description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 10) chain X residue 247 type sequence R description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 11) chain X residue 308 type sequence H description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 12) chain X residue 329 type sequence H description BINDING SITE FOR RESIDUE TLA X 999 source : AC2 13) chain X residue 21 type catalytic sequence G description 194 source MCSA : MCSA1 14) chain X residue 109 type catalytic sequence H description 194 source MCSA : MCSA1 15) chain X residue 110 type catalytic sequence N description 194 source MCSA : MCSA1 16) chain X residue 119 type catalytic sequence I description 194 source MCSA : MCSA1 17) chain X residue 243 type catalytic sequence G description 194 source MCSA : MCSA1 18) chain X residue 245 type catalytic sequence G description 194 source MCSA : MCSA1 19) chain X residue 247 type catalytic sequence R description 194 source MCSA : MCSA1 20) chain X residue 248 type catalytic sequence V description 194 source MCSA : MCSA1 21) chain X residue 330 type catalytic sequence V description 194 source MCSA : MCSA1 22) chain X residue 21 type ACT_SITE sequence G description Proton donor => ECO:0000305|PubMed:23517223 source Swiss-Prot : SWS_FT_FI1 23) chain X residue 109 type ACT_SITE sequence H description Non-phosphorylated intermediate => ECO:0000305|PubMed:11839312, ECO:0000305|PubMed:14725765, ECO:0000305|PubMed:16880541 source Swiss-Prot : SWS_FT_FI2 24) chain X residue 330 type ACT_SITE sequence V description Proton acceptor => ECO:0000305|PubMed:23517223 source Swiss-Prot : SWS_FT_FI3 25) chain X residue 18 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14725765, ECO:0007744|PDB:1PCJ source Swiss-Prot : SWS_FT_FI4 26) chain X residue 309 type BINDING sequence S description BINDING => ECO:0000269|PubMed:14725765, ECO:0007744|PDB:1PCJ source Swiss-Prot : SWS_FT_FI4 27) chain X residue 326 type BINDING sequence M description BINDING => ECO:0000269|PubMed:14725765, ECO:0007744|PDB:1PCJ source Swiss-Prot : SWS_FT_FI4 28) chain X residue 422 type BINDING sequence A description BINDING => ECO:0000269|PubMed:14725765, ECO:0007744|PDB:1PCJ source Swiss-Prot : SWS_FT_FI4 29) chain X residue 109 type BINDING sequence H description via phosphate group => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:23517223 source Swiss-Prot : SWS_FT_FI5 30) chain X residue 243 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:24403075 source Swiss-Prot : SWS_FT_FI6 31) chain X residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:24403075 source Swiss-Prot : SWS_FT_FI6 32) chain X residue 247 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:24403075 source Swiss-Prot : SWS_FT_FI6 33) chain X residue 286 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D, ECO:0007744|PDB:3BKQ source Swiss-Prot : SWS_FT_FI7 34) chain X residue 109 type MOD_RES sequence H description Phosphoserine => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541 source Swiss-Prot : SWS_FT_FI8

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