eF-site ID 1f0x-AB PDB Code 1f0x Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF D-LACTATE DEHYDROGENASE, A PERIPHERAL MEMBRANE RESPIRATORY ENZYME. Classification OXIDOREDUCTASE Compound D-LACTATE DEHYDROGENASE Source Escherichia coli (strain K12) (DLD_ECOLI) Sequence A:  NKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALA VVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPN GNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLE KALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGP AYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDD DRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPD RLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEV LTEIRRHILANFENLPVAGEYMHRDIYDIAELPPRMKNWR DKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPE EGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRN DTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGV DVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFY RENDPTNSMNPGIGKTSKRKNW B:  NKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALA VVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPN GNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLE KALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGP AYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDD DRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPD RLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEV LTEIRRHILANFENLPVAGEYMHRDIYDIAELPPRMKNWR DKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPE EGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRN DTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGV DVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFY RENDPTNSMNPGIGKTSKRKNW Description Functional site 1) chain A residue 39 type sequence F description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 2) chain A residue 73 type sequence L description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 3) chain A residue 74 type sequence M description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 4) chain A residue 76 type sequence A description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 5) chain A residue 77 type sequence A description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 6) chain A residue 78 type sequence N description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 7) chain A residue 79 type sequence T description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 8) chain A residue 80 type sequence G description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 9) chain A residue 81 type sequence L description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 10) chain A residue 84 type sequence G description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 11) chain A residue 85 type sequence S description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 12) chain A residue 142 type sequence I description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 13) chain A residue 143 type sequence G description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 14) chain A residue 144 type sequence S description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 15) chain A residue 150 type sequence S description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 16) chain A residue 152 type sequence I description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 17) chain A residue 156 type sequence C description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 18) chain A residue 159 type sequence S description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 19) chain A residue 160 type sequence G description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 20) chain A residue 257 type sequence A description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 21) chain A residue 258 type sequence G description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 22) chain A residue 260 type sequence L description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 23) chain A residue 262 type sequence V description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 24) chain A residue 528 type sequence E description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 25) chain A residue 529 type sequence H description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 26) chain A residue 555 type sequence N description BINDING SITE FOR RESIDUE FAD A 600 source : AC1 27) chain B residue 1039 type sequence F description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 28) chain B residue 1074 type sequence M description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 29) chain B residue 1076 type sequence A description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 30) chain B residue 1077 type sequence A description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 31) chain B residue 1078 type sequence N description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 32) chain B residue 1079 type sequence T description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 33) chain B residue 1080 type sequence G description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 34) chain B residue 1081 type sequence L description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 35) chain B residue 1084 type sequence G description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 36) chain B residue 1085 type sequence S description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 37) chain B residue 1142 type sequence I description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 38) chain B residue 1143 type sequence G description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 39) chain B residue 1144 type sequence S description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 40) chain B residue 1150 type sequence S description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 41) chain B residue 1152 type sequence I description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 42) chain B residue 1153 type sequence G description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 43) chain B residue 1156 type sequence C description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 44) chain B residue 1159 type sequence S description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 45) chain B residue 1160 type sequence G description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 46) chain B residue 1257 type sequence A description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 47) chain B residue 1258 type sequence G description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 48) chain B residue 1260 type sequence L description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 49) chain B residue 1261 type sequence A description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 50) chain B residue 1262 type sequence V description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 51) chain B residue 1528 type sequence E description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 52) chain B residue 1529 type sequence H description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 53) chain B residue 1555 type sequence N description BINDING SITE FOR RESIDUE FAD B 1600 source : AC2 54) chain A residue 490-496 type prosite sequence FMCYVFH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FMCYVFH source prosite : PS00290 55) chain A residue 76 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 56) chain B residue 1150 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 57) chain B residue 1160 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 58) chain B residue 1262 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 59) chain A residue 84 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 60) chain A residue 143 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 61) chain A residue 150 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 62) chain A residue 160 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 63) chain A residue 262 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 64) chain B residue 1076 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 65) chain B residue 1084 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1 66) chain B residue 1143 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:10944213, ECO:0007744|PDB:1F0X source Swiss-Prot : SWS_FT_FI1

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