eF-site ID 6gy2-ABCD PDB Code 6gy2 Chain A, B, C, D click to enlarge Title Crystal structure of human Plk1-PBD in complex with WSSSLATPPTLSSpTVLI phosphopeptide from BRCA2 Classification CELL CYCLE Compound Serine/threonine-protein kinase PLK1 Source (6GY2) Sequence A:  VDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIF WVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGD SLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEH LLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGS VQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEE YGCCKELASRLRYARTMVDKLLSS B:  DCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFW VSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDS LQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHL LKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSV QINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEY GCCKELASRLRYARTMVDKLLSSR C:  ATPPTLSSXVLI D:  ATPPTLSSXVLI Description Functional site 1) chain A residue 393 type sequence G description binding site for residue GOL A 701 source : AC1 2) chain A residue 394 type sequence L description binding site for residue GOL A 701 source : AC1 3) chain A residue 395 type sequence V description binding site for residue GOL A 701 source : AC1 4) chain A residue 453 type sequence Y description binding site for residue GOL A 701 source : AC1 5) chain A residue 471 type sequence S description binding site for residue GOL A 701 source : AC1 6) chain A residue 475 type sequence K description binding site for residue GOL A 701 source : AC1 7) chain B residue 489 type sequence H description binding site for Ligand residues TPO C 207 through VAL C 208 bound to SER C 206 source : AC2 8) chain B residue 490 type sequence L description binding site for Ligand residues TPO C 207 through VAL C 208 bound to SER C 206 source : AC2 9) chain B residue 491 type sequence L description binding site for Ligand residues TPO C 207 through VAL C 208 bound to SER C 206 source : AC2 10) chain B residue 538 type sequence H description binding site for Ligand residues TPO C 207 through VAL C 208 bound to SER C 206 source : AC2 11) chain B residue 540 type sequence K description binding site for Ligand residues TPO C 207 through VAL C 208 bound to SER C 206 source : AC2 12) chain C residue 206 type sequence S description binding site for Ligand residues TPO C 207 through VAL C 208 bound to SER C 206 source : AC2 13) chain C residue 209 type sequence L description binding site for Ligand residues TPO C 207 through VAL C 208 bound to SER C 206 source : AC2 14) chain A residue 489 type sequence H description binding site for Ligand residues TPO D 207 through VAL D 208 bound to SER D 206 source : AC3 15) chain A residue 490 type sequence L description binding site for Ligand residues TPO D 207 through VAL D 208 bound to SER D 206 source : AC3 16) chain A residue 491 type sequence L description binding site for Ligand residues TPO D 207 through VAL D 208 bound to SER D 206 source : AC3 17) chain A residue 538 type sequence H description binding site for Ligand residues TPO D 207 through VAL D 208 bound to SER D 206 source : AC3 18) chain A residue 540 type sequence K description binding site for Ligand residues TPO D 207 through VAL D 208 bound to SER D 206 source : AC3 19) chain D residue 206 type sequence S description binding site for Ligand residues TPO D 207 through VAL D 208 bound to SER D 206 source : AC3 20) chain D residue 209 type sequence L description binding site for Ligand residues TPO D 207 through VAL D 208 bound to SER D 206 source : AC3 21) chain A residue 375 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 450 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 375 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 450 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 498 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 498 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18691976 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 492 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23455478 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 492 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23455478 source Swiss-Prot : SWS_FT_FI3

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