eF-site ID 5mdh-A PDB Code 5mdh Chain A click to enlarge Title CRYSTAL STRUCTURE OF TERNARY COMPLEX OF PORCINE CYTOPLASMIC MALATE DEHYDROGENASE ALPHA-KETOMALONATE AND TNAD AT 2.4 ANGSTROMS RESOLUTION Classification OXIDOREDUCTASE Compound MALATE DEHYDROGENASE Source Sus scrofa (Pig) (MDHC_PIG) Sequence A:  SEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLL DITPMMGVLDGVLMELQDCALPLLKDVIATDKEEIAFKDL DVAILVGSMPRRDGMERKDLLKANVKIFKCQGAALDKYAK KSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHN RAKAQIALKLGVTSDDVKNVIIWGNHSSTQYPDVNHAKVK LQAKEVGVYEAVKDDSWLKGEFITTVQQRGAAVIKARKLS SAMSAAKAICDHVRDIWFGTPEGEFVSMGIISDGNSYGVP DDLLYSFPVTIKDKTWKIVEGLPINDFSREKMDLTAKELA EEKETAFEFLSSA Description Functional site 1) chain A residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 2) chain A residue 12 type sequence A description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 3) chain A residue 13 type sequence G description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 4) chain A residue 14 type sequence Q description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 5) chain A residue 15 type sequence I description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 6) chain A residue 41 type sequence D description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 7) chain A residue 86 type sequence V description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 8) chain A residue 87 type sequence G description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 9) chain A residue 88 type sequence S description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 10) chain A residue 89 type sequence M description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 11) chain A residue 90 type sequence P description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 12) chain A residue 107 type sequence I description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 13) chain A residue 128 type sequence V description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 14) chain A residue 129 type sequence G description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 15) chain A residue 130 type sequence N description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 16) chain A residue 154 type sequence L description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 17) chain A residue 186 type sequence H description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 18) chain A residue 240 type sequence S description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 19) chain A residue 241 type sequence S description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 20) chain A residue 245 type sequence A description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 21) chain A residue 91 type sequence R description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 22) chain A residue 97 type sequence R description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 23) chain A residue 130 type sequence N description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 24) chain A residue 157 type sequence L description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 25) chain A residue 161 type sequence R description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 26) chain A residue 186 type sequence H description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 27) chain A residue 234 type sequence I description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 28) chain A residue 241 type sequence S description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 29) chain A residue 159 type catalytic sequence H description 526 source MCSA : MCSA1 30) chain A residue 187 type catalytic sequence S description 526 source MCSA : MCSA1 31) chain A residue 154-166 type prosite sequence LTRLDHNRAKAQI description MDH Malate dehydrogenase active site signature. LTRLDhnRAkaqI source prosite : PS00068 32) chain A residue 187 type ACT_SITE sequence S description Proton acceptor => ECO:0000305|PubMed:2775751 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10 34) chain A residue 333 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10 35) chain A residue 298 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI11 36) chain A residue 332 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88989 source Swiss-Prot : SWS_FT_FI12 37) chain A residue 11 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 42 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 129 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 92 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 98 type BINDING sequence K description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 131 type BINDING sequence P description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 162 type BINDING sequence A description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 105 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 112 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 2 type MOD_RES sequence E description N-acetylserine => ECO:0000269|PubMed:3606987 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 110 type MOD_RES sequence C description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 48) chain A residue 214 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 49) chain A residue 318 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 118 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 51) chain A residue 121 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 52) chain A residue 217 type MOD_RES sequence W description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 53) chain A residue 309 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 54) chain A residue 230 type MOD_RES sequence G description Omega-N-methylarginine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI9

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