eF-site ID 5mdh-B PDB Code 5mdh Chain 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 B:  SEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLL DITPMMGVLDGVLMELQDCALPLLKDVIATDKEEIAFKDL DVAILVGSMPRRDGMERKDLLKANVKIFKCQGAALDKYAK KSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHN RAKAQIALKLGVTSDDVKNVIIWGNHSSTQYPDVNHAKVK LQAKEVGVYEAVKDDSWLKGEFITTVQQRGAAVIKARKLS SAMSAAKAICDHVRDIWFGTPEGEFVSMGIISDGNSYGVP DDLLYSFPVTIKDKTWKIVEGLPINDFSREKMDLTAKELA EEKETAFEFLSSA Description Functional site 1) chain B residue 301 type sequence G description BINDING SITE FOR RESIDUE NAD A 334 source : AC1 2) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 3) chain B residue 13 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 4) chain B residue 14 type sequence Q description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 5) chain B residue 15 type sequence I description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 6) chain B residue 41 type sequence D description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 7) chain B residue 42 type sequence I description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 8) chain B residue 86 type sequence V description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 9) chain B residue 87 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 10) chain B residue 88 type sequence S description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 11) chain B residue 107 type sequence I description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 12) chain B residue 111 type sequence Q description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 13) chain B residue 128 type sequence V description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 14) chain B residue 129 type sequence G description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 15) chain B residue 130 type sequence N description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 16) chain B residue 154 type sequence L description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 17) chain B residue 157 type sequence L description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 18) chain B residue 186 type sequence H description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 19) chain B residue 240 type sequence S description BINDING SITE FOR RESIDUE NAD B 334 source : AC3 20) chain B residue 157 type sequence L description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 21) chain B residue 158 type sequence D description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 22) chain B residue 161 type sequence R description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 23) chain B residue 186 type sequence H description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 24) chain B residue 230 type sequence G description BINDING SITE FOR RESIDUE MAK B 335 source : AC4 25) chain B residue 2 type MOD_RES sequence E description N-acetylserine => ECO:0000269|PubMed:3606987 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 110 type MOD_RES sequence C description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 27) chain B residue 214 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 28) chain B residue 318 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI6 29) chain B residue 118 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 30) chain B residue 121 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI7 31) chain B residue 217 type MOD_RES sequence W description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 32) chain B residue 309 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI8 33) chain B residue 230 type MOD_RES sequence G description Omega-N-methylarginine => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI9 34) chain B residue 298 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P14152 source Swiss-Prot : SWS_FT_FI11 35) chain B residue 332 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88989 source Swiss-Prot : SWS_FT_FI12 36) chain B residue 159 type catalytic sequence H description 526 source MCSA : MCSA2 37) chain B residue 187 type catalytic sequence S description 526 source MCSA : MCSA2 38) chain B residue 187 type ACT_SITE sequence S description Proton acceptor => ECO:0000305|PubMed:2775751 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 11 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 42 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 129 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524, ECO:0000269|PubMed:2775751 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 92 type BINDING sequence R description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 43) chain B residue 98 type BINDING sequence K description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 44) chain B residue 131 type BINDING sequence P description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 162 type BINDING sequence A description BINDING => ECO:0000305|PubMed:10075524 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 105 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 47) chain B residue 112 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10075524 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10 49) chain B residue 333 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40925 source Swiss-Prot : SWS_FT_FI10

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