eF-site ID 1v3u-AB PDB Code 1v3u Chain A, B click to enlarge Title Crystal structure of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase in apo form Classification OXIDOREDUCTASE Compound leukotriene b4 12-hydroxydehydrogenase/prostaglandin 15-keto reductase Source Cavia porcellus (Guinea pig) (Q9EQZ5_CAVPO) Sequence A:  FMVKAKSWTLKKPTQSDFELKTVELPPLKNGEVLLEALFL SVDPYMRIASKRLKEGAVMMGQQVARVVESKNSAFPAGSI VLAQSGWTTHFISDGKGLEKLLWPDKLPLSLALGTIGMPG LTAYFGLLEVCGVKGGETVLVSAAAGAVGSVVGQIAKLKG CKVVGAAGSDEKIAYLKQIGFDAAFNYKTVNSLEEALKKA SPDGYDCYFDNVGGEFLNTVLSQMKDFGKIAICGAISLPP GPSPESIIYKQLRIEGFIVYRWQGDVREKALRDLMKWVLE GKIQYHEHVTKGFENMPAAFIEMLNGANLGKAVVTA B:  PEFMVKAKSWTLKKHFQGKPTQSDFELKTVELPPLKNGEV LLEALFLSVDPYMRIASKRLKEGAVMMGQQVARVVESKNS AFPAGSIVLAQSGWTTHFISDGKGLEKLLTEWPDKLPLSL ALGTIGMPGLTAYFGLLEVCGVKGGETVLVSAAAGAVGSV VGQIAKLKGCKVVGAAGSDEKIAYLKQIGFDAAFNYKTVN SLEEALKKASPDGYDCYFDNVGGEFLNTVLSQMKDFGKIA ICGAISVYNRMDQLPPGPSPESIIYKQLRIEGFIVYRWQG DVREKALRDLMKWVLEGKIQYHEHVTKGFENMPAAFIEML NGANLGKAVVTA Description Functional site 1) chain A residue 324 type sequence K description BINDING SITE FOR RESIDUE CL A 1001 source : AC1 2) chain A residue 325 type sequence A description BINDING SITE FOR RESIDUE CL A 1001 source : AC1 3) chain B residue 149 type sequence A description BINDING SITE FOR RESIDUE CL B 1002 source : AC2 4) chain B residue 151 type sequence A description BINDING SITE FOR RESIDUE CL B 1002 source : AC2 5) chain B residue 173 type sequence A description BINDING SITE FOR RESIDUE CL B 1002 source : AC2 6) chain B residue 174 type sequence G description BINDING SITE FOR RESIDUE CL B 1002 source : AC2 7) chain B residue 178 type sequence K description BINDING SITE FOR RESIDUE CL B 1002 source : AC2 8) chain B residue 12 type sequence H description BINDING SITE FOR RESIDUE CL B 1003 source : AC3 9) chain B residue 13 type sequence F description BINDING SITE FOR RESIDUE CL B 1003 source : AC3 10) chain B residue 54 type sequence S description BINDING SITE FOR RESIDUE CL B 1003 source : AC3 11) chain B residue 55 type sequence K description BINDING SITE FOR RESIDUE CL B 1003 source : AC3 12) chain A residue 70 type sequence R description BINDING SITE FOR RESIDUE CL A 1004 source : AC4 13) chain A residue 72 type sequence V description BINDING SITE FOR RESIDUE CL A 1004 source : AC4 14) chain B residue 321 type sequence N description BINDING SITE FOR RESIDUE CL B 1005 source : AC5 15) chain B residue 324 type sequence K description BINDING SITE FOR RESIDUE CL B 1005 source : AC5 16) chain B residue 325 type sequence A description BINDING SITE FOR RESIDUE CL B 1005 source : AC5 17) chain A residue 149 type sequence A description BINDING SITE FOR RESIDUE CL A 1006 source : AC6 18) chain A residue 151 type sequence A description BINDING SITE FOR RESIDUE CL A 1006 source : AC6 19) chain A residue 173 type sequence A description BINDING SITE FOR RESIDUE CL A 1006 source : AC6 20) chain A residue 178 type sequence K description BINDING SITE FOR RESIDUE CL A 1006 source : AC6 21) chain B residue 12 type sequence H description BINDING SITE FOR RESIDUE CL B 1007 source : AC7 22) chain B residue 59 type sequence E description BINDING SITE FOR RESIDUE CL B 1007 source : AC7 23) chain A residue 152 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 193 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 217 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 239 type BINDING sequence C description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 270 type BINDING sequence F description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 321 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 178 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 193 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 217 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 239 type BINDING sequence C description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 270 type BINDING sequence F description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 321 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 152 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 178 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15007077 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 18 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q14914 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 18 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q14914 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 20 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q14914 source Swiss-Prot : SWS_FT_FI3 40) chain B residue 20 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q14914 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 178 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q91YR9 source Swiss-Prot : SWS_FT_FI4 42) chain B residue 178 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q91YR9 source Swiss-Prot : SWS_FT_FI4

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