eF-site ID 5mdh-AB PDB Code 5mdh Chain A, B 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 B:  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 B residue 301 type sequence G description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 22) chain A residue 91 type sequence R description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 23) chain A residue 97 type sequence R description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 24) chain A residue 130 type sequence N description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 25) chain A residue 157 type sequence L description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 26) chain A residue 161 type sequence R description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 27) chain A residue 186 type sequence H description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 28) chain A residue 234 type sequence I description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 29) chain A residue 241 type sequence S description BINDING SITE FOR RESIDUE MAK A 335 source : AC2 30) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 31) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 32) chain B residue 14 type sequence Q description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 33) chain B residue 15 type sequence I description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 34) chain B residue 41 type sequence D description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 35) chain B residue 42 type sequence I description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 36) chain B residue 86 type sequence V description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 37) chain B residue 87 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 38) chain B residue 88 type sequence S description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 39) chain B residue 107 type sequence I description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 40) chain B residue 111 type sequence Q description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 41) chain B residue 128 type sequence V description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 42) chain B residue 129 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 43) chain B residue 130 type sequence N description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 44) chain B residue 154 type sequence L description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 45) chain B residue 157 type sequence L description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 46) chain B residue 186 type sequence H description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 47) chain B residue 240 type sequence S description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 48) chain B residue 157 type sequence L description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 49) chain B residue 158 type sequence D description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 50) chain B residue 161 type sequence R description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 51) chain B residue 186 type sequence H description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 52) chain B residue 230 type sequence G description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 53) chain A residue 159 type catalytic sequence H description 526 source MCSA : MCSA1 54) chain A residue 187 type catalytic sequence S description 526 source MCSA : MCSA1 55) chain B residue 159 type catalytic sequence H description 526 source MCSA : MCSA2 56) chain B residue 187 type catalytic sequence S description 526 source MCSA : MCSA2 57) chain A residue 154-166 type prosite sequence LTRLDHNRAKAQI description MDH Malate dehydrogenase active site signature. LTRLDhnRAkaqI source prosite : PS00068 58) chain A residue 187 type ACT_SITE sequence S description Proton acceptor => ECO:0000305|PubMed:2775751 source Swiss-Prot : SWS_FT_FI1 59) chain B residue 187 type ACT_SITE sequence S description Proton acceptor => ECO:0000305|PubMed:2775751 source Swiss-Prot : SWS_FT_FI1 60) chain A residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10 61) chain A residue 333 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10 62) chain B residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10 63) chain B residue 333 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10 64) chain A residue 298 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI11 65) chain B residue 298 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI11 66) chain A residue 332 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88989 source Swiss-Prot : SWS_FT_FI12 67) chain B residue 332 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88989 source Swiss-Prot : SWS_FT_FI12 68) chain A residue 11 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 42 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 70) chain A residue 129 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 71) chain B residue 11 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 72) chain B residue 42 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 73) chain B residue 129 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 74) chain A residue 92 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 75) chain A residue 98 type BINDING sequence K description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 76) chain A residue 131 type BINDING sequence P description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 77) chain A residue 162 type BINDING sequence A description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 78) chain B residue 92 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 79) chain B residue 98 type BINDING sequence K description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 80) chain B residue 131 type BINDING sequence P description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 81) chain B residue 162 type BINDING sequence A description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 82) chain A residue 105 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 83) chain A residue 112 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 84) chain B residue 105 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 85) chain B residue 112 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 86) chain A residue 2 type MOD_RES sequence E description N-acetylserine => ECO:0000269|PubMed:3606987 source Swiss-Prot : SWS_FT_FI5 87) chain B residue 2 type MOD_RES sequence E description N-acetylserine => ECO:0000269|PubMed:3606987 source Swiss-Prot : SWS_FT_FI5 88) chain A residue 110 type MOD_RES sequence C description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 89) chain A residue 214 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 90) chain A residue 318 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 91) chain B residue 110 type MOD_RES sequence C description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 92) chain B residue 214 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 93) chain B residue 318 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 94) chain A residue 118 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 95) chain A residue 121 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 96) chain B residue 118 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 97) chain B residue 121 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 98) chain A residue 217 type MOD_RES sequence W description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 99) chain A residue 309 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 100) chain B residue 217 type MOD_RES sequence W description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 101) chain B residue 309 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 102) chain A residue 230 type MOD_RES sequence G description Omega-N-methylarginine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI9 103) chain B 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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