eF-site ID 6b1c-ABC PDB Code 6b1c Chain A, B, C click to enlarge Title Macrophage Migration Inhibitory Factor in complex with a Naphthyridinone Inhibitor (4a) Classification ISOMERASE/ISOMERASE inhibitor Compound Macrophage migration inhibitory factor Source (MIF_HUMAN) Sequence A:  PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVH VVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLC GLLAERLRISPDRVYINYYDMNAANVGWNNSTFA B:  PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVH VVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLC GLLAERLRISPDRVYINYYDMNAANVGWNNSTFA C:  PMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVH VVPDQLMAFGGSSEPCALCSLHSIGKIGGAQNRSYSKLLC GLLAERLRISPDRVYINYYDMNAANVGWNNSTFA Description Functional site 1) chain A residue 68 type sequence G description binding site for residue SO4 A 201 source : AC1 2) chain A residue 69 type sequence G description binding site for residue SO4 A 201 source : AC1 3) chain A residue 70 type sequence A description binding site for residue SO4 A 201 source : AC1 4) chain A residue 71 type sequence Q description binding site for residue SO4 A 201 source : AC1 5) chain A residue 1 type sequence P description binding site for residue C9J A 202 source : AC2 6) chain A residue 2 type sequence M description binding site for residue C9J A 202 source : AC2 7) chain A residue 32 type sequence K description binding site for residue C9J A 202 source : AC2 8) chain A residue 36 type sequence Y description binding site for residue C9J A 202 source : AC2 9) chain A residue 62 type sequence H description binding site for residue C9J A 202 source : AC2 10) chain A residue 63 type sequence S description binding site for residue C9J A 202 source : AC2 11) chain A residue 64 type sequence I description binding site for residue C9J A 202 source : AC2 12) chain A residue 101 type sequence M description binding site for residue C9J A 202 source : AC2 13) chain A residue 106 type sequence V description binding site for residue C9J A 202 source : AC2 14) chain B residue 92 type sequence D description binding site for residue C9J A 202 source : AC2 15) chain C residue 95 type sequence Y description binding site for residue C9J A 202 source : AC2 16) chain C residue 97 type sequence N description binding site for residue C9J A 202 source : AC2 17) chain A residue 95 type sequence Y description binding site for residue C9J B 201 source : AC3 18) chain A residue 97 type sequence N description binding site for residue C9J B 201 source : AC3 19) chain B residue 1 type sequence P description binding site for residue C9J B 201 source : AC3 20) chain B residue 2 type sequence M description binding site for residue C9J B 201 source : AC3 21) chain B residue 32 type sequence K description binding site for residue C9J B 201 source : AC3 22) chain B residue 36 type sequence Y description binding site for residue C9J B 201 source : AC3 23) chain B residue 62 type sequence H description binding site for residue C9J B 201 source : AC3 24) chain B residue 63 type sequence S description binding site for residue C9J B 201 source : AC3 25) chain B residue 64 type sequence I description binding site for residue C9J B 201 source : AC3 26) chain B residue 101 type sequence M description binding site for residue C9J B 201 source : AC3 27) chain B residue 106 type sequence V description binding site for residue C9J B 201 source : AC3 28) chain B residue 113 type sequence F description binding site for residue C9J B 201 source : AC3 29) chain A residue 77 type sequence K description binding site for residue SO4 C 201 source : AC4 30) chain C residue 16 type sequence D description binding site for residue SO4 C 201 source : AC4 31) chain C residue 17 type sequence G description binding site for residue SO4 C 201 source : AC4 32) chain C residue 18 type sequence F description binding site for residue SO4 C 201 source : AC4 33) chain C residue 19 type sequence L description binding site for residue SO4 C 201 source : AC4 34) chain C residue 20 type sequence S description binding site for residue SO4 C 201 source : AC4 35) chain C residue 68 type sequence G description binding site for residue SO4 C 202 source : AC5 36) chain C residue 69 type sequence G description binding site for residue SO4 C 202 source : AC5 37) chain C residue 70 type sequence A description binding site for residue SO4 C 202 source : AC5 38) chain C residue 71 type sequence Q description binding site for residue SO4 C 202 source : AC5 39) chain A residue 73 type sequence R description binding site for residue SO4 C 203 source : AC6 40) chain C residue 15 type sequence P description binding site for residue SO4 C 203 source : AC6 41) chain C residue 16 type sequence D description binding site for residue SO4 C 203 source : AC6 42) chain A residue 1 type ACT_SITE sequence P description Proton acceptor; via imino nitrogen => ECO:0000250|UniProtKB:P34884 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 1 type ACT_SITE sequence P description Proton acceptor; via imino nitrogen => ECO:0000250|UniProtKB:P34884 source Swiss-Prot : SWS_FT_FI1 44) chain C residue 1 type ACT_SITE sequence P description Proton acceptor; via imino nitrogen => ECO:0000250|UniProtKB:P34884 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 54-68 type prosite sequence EPCALCSLHSIGKIG description MIF Macrophage migration inhibitory factor family signature. EPCAlcsLhSIGkIG source prosite : PS01158 46) chain A residue 32 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 64 type BINDING sequence I description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 97 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 32 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 64 type BINDING sequence I description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 97 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 32 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 53) chain C residue 64 type BINDING sequence I description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 54) chain C residue 97 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11170644, ECO:0000269|PubMed:17526494, ECO:0000269|PubMed:19090677 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 77 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P34884 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P34884 source Swiss-Prot : SWS_FT_FI3 57) chain C residue 77 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P34884 source Swiss-Prot : SWS_FT_FI3

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