eF-site ID 1ndh-A PDB Code 1ndh Chain A click to enlarge Title CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION Classification ELECTRON TRANSPORT (FLAVO PROTEIN) Compound CYTOCHROME B5 REDUCTASE Source (NCB5R_PIG) Sequence A:  PAITLENPDIKYPLRLIDKEVVNHDTRRFRFALPSPEHIL GLPVGQHIYLSARIDGNLVIRPYTPVSSDDDKGFVDLVIK VYFKDTHPKFPAGGKMSQYLESMKIGDTIEFRGPNGLLVY QGKGKFAIRPDKKSSPVIKTVKSVGMIAGGTGITPMLQVI RAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNEHSA RFKLWYTVDRAPEAWDYSQGFVNEEMIRDHLPPPEEEPLV LMCGPPPMIQYACLPNLERVGHPKERCFAF Description Functional site 1) chain A residue 63 type sequence R description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 2) chain A residue 64 type sequence P description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 3) chain A residue 65 type sequence Y description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 4) chain A residue 66 type sequence T description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 5) chain A residue 81 type sequence I description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 6) chain A residue 82 type sequence K description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 7) chain A residue 83 type sequence V description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 8) chain A residue 85 type sequence F description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 9) chain A residue 86 type sequence K description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 10) chain A residue 91 type sequence K description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 11) chain A residue 95 type sequence G description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 12) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 13) chain A residue 97 type sequence K description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 14) chain A residue 98 type sequence M description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 15) chain A residue 99 type sequence S description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 16) chain A residue 153 type sequence T description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 17) chain A residue 156 type sequence T description BINDING SITE FOR RESIDUE FAD A 273 source : AC1 18) chain A residue 21 type catalytic sequence K description 862 source MCSA : MCSA1 19) chain A residue 37 type catalytic sequence S description 862 source MCSA : MCSA1 20) chain A residue 38 type catalytic sequence P description 862 source MCSA : MCSA1 21) chain A residue 217 type catalytic sequence W description 862 source MCSA : MCSA1 22) chain A residue 63 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCN2 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 35 type BINDING sequence L description BINDING => ECO:0000269|PubMed:7893687, ECO:0007744|PDB:1NDH source Swiss-Prot : SWS_FT_FI1 24) chain A residue 36 type BINDING sequence P description BINDING => ECO:0000269|PubMed:7893687, ECO:0007744|PDB:1NDH source Swiss-Prot : SWS_FT_FI1 25) chain A residue 37 type BINDING sequence S description BINDING => ECO:0000269|PubMed:7893687, ECO:0007744|PDB:1NDH source Swiss-Prot : SWS_FT_FI1 26) chain A residue 69 type BINDING sequence S description BINDING => ECO:0000269|PubMed:7893687, ECO:0007744|PDB:1NDH source Swiss-Prot : SWS_FT_FI1 27) chain A residue 70 type BINDING sequence S description BINDING => ECO:0000269|PubMed:7893687, ECO:0007744|PDB:1NDH source Swiss-Prot : SWS_FT_FI1 28) chain A residue 71 type BINDING sequence D description BINDING => ECO:0000269|PubMed:7893687, ECO:0007744|PDB:1NDH source Swiss-Prot : SWS_FT_FI1 29) chain A residue 52 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00387 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 54 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P00387 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 56 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P00387 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 128 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P00387 source Swiss-Prot : SWS_FT_FI2

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