eF-site ID 3d2r-AB PDB Code 3d2r Chain A, B click to enlarge Title Crystal structure of pyruvate dehydrogenase kinase isoform 4 in complex with ADP Classification TRANSFERASE Compound [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4 Source Homo sapiens (Human) (PDK4_HUMAN) Sequence A:  PREVEHFSRYSPSPLSMKQLLDFGSENCERTSFAFLRQEL PVRLANILKEIDILPTQLVNTSSVQLVKSWYIQSLMDLVE FHEKSPDDQKALSDFVDTLIKVRNRHHNVVPTMAQGIIEY KDACDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDS HIGSIDPNCDVVAVVQDAFECSRMLCDQYYLSSPELKLTQ VNGKFPDQPIHIVYVPSHLHHMLFELFKNAMRATVEHQEN QPSLTPIEVIVVLGKEDLTIKISDRGGGVPLRIIDRLFSY TYSTAPTAPLAGFGYGLPISRLYAKYFQGDLNLYSLSGYG TDAIIYLKALSSESIEKLPVFNKSAFKHYDDWCI B:  VPREVEHFSRYSPSPLSMKQLLDFGSENACERTSFAFLRQ ELPVRLANILKEIDILPTQLVNTSSVQLVKSWYIQSLMDL VEFHEKSPDDQKALSDFVDTLIKVRNRHHNVVPTMAQGII EYKACTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIF SDSQTGNPSHIGSIDPNCDVVAVVQDAFECSRMLCDQYYL SSPELKLTQVNGKFPDQPIHIVYVPSHLHHMLFELFKNAM RATVEHQENQPSLTPIEVIVVLGKEDLTIKISDRGGGVPL RIIDRLFSYTYSTAPTPPLAGFGYGLPISRLYAKYFQGDL NLYSLSGYGTDAIIYLKALSSESIEKLPVFNKSAFKHYDW CI Description Functional site 1) chain A residue 258 type sequence N description BINDING SITE FOR RESIDUE MG A 500 source : AC1 2) chain B residue 258 type sequence N description BINDING SITE FOR RESIDUE MG B 500 source : AC2 3) chain A residue 258 type sequence N description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 4) chain A residue 261 type sequence R description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 5) chain A residue 262 type sequence A description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 6) chain A residue 293 type sequence D description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 7) chain A residue 306 type sequence L description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 8) chain A residue 311 type sequence Y description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 9) chain A residue 312 type sequence S description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 10) chain A residue 313 type sequence T description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 11) chain A residue 328 type sequence A description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 12) chain A residue 329 type sequence G description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 13) chain A residue 330 type sequence F description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 14) chain A residue 331 type sequence G description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 15) chain A residue 333 type sequence G description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 16) chain A residue 334 type sequence L description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 17) chain A residue 358 type sequence T description BINDING SITE FOR RESIDUE ADP A 501 source : AC3 18) chain B residue 258 type sequence N description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 19) chain B residue 261 type sequence R description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 20) chain B residue 262 type sequence A description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 21) chain B residue 293 type sequence D description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 22) chain B residue 306 type sequence L description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 23) chain B residue 311 type sequence Y description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 24) chain B residue 312 type sequence S description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 25) chain B residue 313 type sequence T description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 26) chain B residue 328 type sequence A description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 27) chain B residue 329 type sequence G description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 28) chain B residue 330 type sequence F description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 29) chain B residue 331 type sequence G description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 30) chain B residue 333 type sequence G description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 31) chain B residue 334 type sequence L description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 32) chain B residue 358 type sequence T description BINDING SITE FOR RESIDUE ADP B 501 source : AC4 33) chain A residue 160 type sequence D description BINDING SITE FOR RESIDUE GOL A 502 source : AC5 34) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE GOL A 502 source : AC5 35) chain A residue 374 type sequence K description BINDING SITE FOR RESIDUE GOL A 502 source : AC5 36) chain B residue 395 type sequence W description BINDING SITE FOR RESIDUE GOL A 502 source : AC5 37) chain A residue 395 type sequence W description BINDING SITE FOR RESIDUE GOL B 502 source : AC6 38) chain B residue 160 type sequence D description BINDING SITE FOR RESIDUE GOL B 502 source : AC6 39) chain B residue 339 type sequence L description BINDING SITE FOR RESIDUE GOL B 502 source : AC6 40) chain B residue 342 type sequence K description BINDING SITE FOR RESIDUE GOL B 502 source : AC6 41) chain B residue 374 type sequence K description BINDING SITE FOR RESIDUE GOL B 502 source : AC6 42) chain A residue 254 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 293 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 312 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 329 type BINDING sequence G description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 254 type BINDING sequence E description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 293 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 312 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 329 type BINDING sequence G description BINDING => ECO:0000269|PubMed:18658136 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 157 type SITE sequence Y description Interaction with the other subunit in the homodimer source Swiss-Prot : SWS_FT_FI2 51) chain A residue 161 type SITE sequence R description Interaction with the other subunit in the homodimer source Swiss-Prot : SWS_FT_FI2 52) chain A residue 395 type SITE sequence W description Interaction with the other subunit in the homodimer source Swiss-Prot : SWS_FT_FI2 53) chain B residue 157 type SITE sequence Y description Interaction with the other subunit in the homodimer source Swiss-Prot : SWS_FT_FI2 54) chain B residue 161 type SITE sequence R description Interaction with the other subunit in the homodimer source Swiss-Prot : SWS_FT_FI2 55) chain B residue 395 type SITE sequence W description Interaction with the other subunit in the homodimer source Swiss-Prot : SWS_FT_FI2

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