eF-site ID 3cr3-ABCD PDB Code 3cr3 Chain A, B, C, D click to enlarge Title Structure of a transient complex between Dha-kinase subunits DhaM and DhaL from Lactococcus lactis Classification TRANSFERASE Compound PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL Source Lactococcus lactis subsp. lactis (Streptococcus lactis) (DHAM_LACLA) Sequence A:  LLTIDTTIEWLGKFNEKIQENKAYLSELDGPIGDGDHGAN XARGXSETXKALEVSNFGNVSEIFKKVAXTLXSKVGGASG PLYGSAFLAXSKTAIETLDTSELIYAGLEAIQKRGKAQVG EKTXVDIWSAFLNDLQTDSASKDNLEKVVKASAGLLATKG RASYLGERSIGHIDPGTQSSAYLFETLLEVVA B:  LLTIDTTIEWLGKFNEKIQENKAYLSELDGPIGDGDHGAN XARGXSETXKALEVSNFGNVSEIFKKVAXTLXSKVGGASG PLYGSAFLAXSKTAIETLDTSELIYAGLEAIQKRGKAQVG EKTXVDIWSAFLNDLQTDSASKDNLEKVVKASAGLLATKG RASYLGERSIGHIDPGTQSSAYLFETLLEVVA C:  YGIVIVSHSPEIASGLKKLIREVAKNISLTAIGGLENGEI GTSFDRVXNAIEENEADNLLTFFDLGSARXNLDLVSEXTD KELTIFNVPLIEGAYTASALLEAGATFEAIKEQLEKXLIE K D:  YGIVIVSHSPEIASGLKKLIREVAKNISLTAIGGLENGEI GTSFDRVXNAIEENEADNLLTFFDLGSARXNLDLVSEXTD KELTIFNVPLIEGAYTASALLEAGATFEAIKEQLEKXLIE K Description (1)  PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL, PTS-dependent dihydroxyacetone kinase, phosphotransferase subunit dhaM Functional site 1) chain B residue 29 type sequence D description BINDING SITE FOR RESIDUE MG B 1212 source : AC1 2) chain B residue 34 type sequence D description BINDING SITE FOR RESIDUE MG B 1212 source : AC1 3) chain B residue 36 type sequence D description BINDING SITE FOR RESIDUE MG B 1212 source : AC1 4) chain B residue 34 type sequence D description BINDING SITE FOR RESIDUE MG B 1213 source : AC2 5) chain B residue 36 type sequence D description BINDING SITE FOR RESIDUE MG B 1213 source : AC2 6) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE MG A 1212 source : AC3 7) chain A residue 34 type sequence D description BINDING SITE FOR RESIDUE MG A 1212 source : AC3 8) chain A residue 36 type sequence D description BINDING SITE FOR RESIDUE MG A 1212 source : AC3 9) chain A residue 34 type sequence D description BINDING SITE FOR RESIDUE MG A 1213 source : AC4 10) chain A residue 36 type sequence D description BINDING SITE FOR RESIDUE MG A 1213 source : AC4 11) chain B residue 29 type sequence D description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 12) chain B residue 34 type sequence D description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 13) chain B residue 36 type sequence D description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 14) chain B residue 37 type sequence H description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 15) chain B residue 40 type sequence N description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 16) chain B residue 77 type sequence G description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 17) chain B residue 78 type sequence A description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 18) chain B residue 79 type sequence S description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 19) chain B residue 82 type sequence L description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 20) chain B residue 115 type sequence G description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 21) chain B residue 117 type sequence A description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 22) chain B residue 123 type sequence T description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 23) chain B residue 160 type sequence G description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 24) chain B residue 161 type sequence R description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 25) chain B residue 174 type sequence D description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 26) chain B residue 175 type sequence P description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 27) chain B residue 176 type sequence G description BINDING SITE FOR RESIDUE ADP B 1211 source : AC5 28) chain A residue 29 type sequence D description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 29) chain A residue 34 type sequence D description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 30) chain A residue 36 type sequence D description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 31) chain A residue 37 type sequence H description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 32) chain A residue 40 type sequence N description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 33) chain A residue 77 type sequence G description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 34) chain A residue 78 type sequence A description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 35) chain A residue 79 type sequence S description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 36) chain A residue 82 type sequence L description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 37) chain A residue 115 type sequence G description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 38) chain A residue 117 type sequence A description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 39) chain A residue 123 type sequence T description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 40) chain A residue 160 type sequence G description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 41) chain A residue 161 type sequence R description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 42) chain A residue 174 type sequence D description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 43) chain A residue 175 type sequence P description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 44) chain A residue 176 type sequence G description BINDING SITE FOR RESIDUE ADP A 1211 source : AC6 45) chain C residue 10 type ACT_SITE sequence H description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 34 type ACT_SITE sequence D description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 36 type ACT_SITE sequence D description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 37 type ACT_SITE sequence H description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 78 type ACT_SITE sequence A description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 115 type ACT_SITE sequence G description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 124 type ACT_SITE sequence X description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 174 type ACT_SITE sequence D description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 53) chain D residue 10 type ACT_SITE sequence H description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 36 type ACT_SITE sequence D description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 37 type ACT_SITE sequence H description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 78 type ACT_SITE sequence A description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 115 type ACT_SITE sequence G description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 124 type ACT_SITE sequence X description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 174 type ACT_SITE sequence D description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 60) chain B residue 29 type ACT_SITE sequence D description Tele-phosphohistidine intermediate; for EIIA activity => ECO:0000255|PROSITE-ProRule:PRU00419 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 161 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18957416 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 161 type BINDING sequence R description BINDING => ECO:0000305|PubMed:18957416 source Swiss-Prot : SWS_FT_FI2

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