eF-site ID 1eyy-ABCD PDB Code 1eyy Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURE OF THE NADP+ DEPENDENT ALDEHYDE DEHYDROGENASE FROM VIBRIO HARVEYI. Classification OXIDOREDUCTASE Compound ALDEHYDE DEHYDROGENASE Source null (ALDH_VIBHA) Sequence A:  TDNVFYATNAFTGEALPLAFPVHTEVEVNQAATAAAKVAR DFRRLNNSKRASLLRTIASELEARSDDIIARAHLETALPE VRLTGEIARTANQLRLFADVVNSGSYHQAILDTPNPTRAP LPKPDIRRQQIALGPVAVFGASNFPLAFSAAGGDTASALA AGCPVIVKGHTAHPGTSQIVAECIEQALKQEQLPQAIFTL LQGNQRALGQALVSHPEIKAVGFTGSVGGGRALFNLAHER PEPIPFYGELGAINPTFIFPSAMRAKADLADQFVASMTMG CGQFCTKPGVVFALNTPETQAFIETAQSLIRQQSPSTLLT PGIRDSYQSQVVSRGSDDGIDVTFSQAESPCVASALFVTS SENWRKHPAWEEEIFGPQSLIVVCENVADMLSLSEMLAGS LTATIHATEEDYPQVSQLIPRLEEIAGRLVFNGWPTGVEV GYAMVHGGPYPASTHSASTSVGAEAIHRWLRPVAYQALPE SLLPDSLKAENPLEIARAVDGKAA B:  NVFYATNAFTGEALPLAFPVHTEVEVNQAATAAAKVARDF RRLNNSKRASLLRTIASELEARSDDIIARAHLETALPEVR LTGEIARTANQLRLFADVVNSGSYHQAILDTPNPTRAPLP KPDIRRQQIALGPVAVFGASNFPLAFSAAGGDTASALAAG CPVIVKGHTAHPGTSQIVAECIEQALKQEQLPQAIFTLLQ GNQRALGQALVSHPEIKAVGFTGSVGGGRALFNLAHERPE PIPFYGELGAINPTFIFPSAMRAKADLADQFVASMTMGCG QFCTKPGVVFALNTPETQAFIETAQSLIRQQSPSTLLTPG IRDSYQSQVVSRGSDDGIDVTFSQAESPCVASALFVTSSE NWRKHPAWEEEIFGPQSLIVVCENVADMLSLSEMLAGSLT ATIHATEEDYPQVSQLIPRLEEIAGRLVFNGWPTGVEVGY AMVHGGPYPASTHSASTSVGAEAIHRWLRPVAYQALPESL LPDSLKAENPLEIARAVDGKAA C:  NVFYATNAFTGEALPLAFPVHTEVEVNQAATAAAKVARDF RRLNNSKRASLLRTIASELEARSDDIIARAHLETALPEVR LTGEIARTANQLRLFADVVNSGSYHQAILDTPNPTRAPLP KPDIRRQQIALGPVAVFGASNFPLAFSAAGGDTASALAAG CPVIVKGHTAHPGTSQIVAECIEQALKQEQLPQAIFTLLQ GNQRALGQALVSHPEIKAVGFTGSVGGGRALFNLAHERPE PIPFYGELGAINPTFIFPSAMRAKADLADQFVASMTMGCG QFCTKPGVVFALNTPETQAFIETAQSLIRQQSPSTLLTPG IRDSYQSQVVSRGSDDGIDVTFSQAESPCVASALFVTSSE NWRKHPAWEEEIFGPQSLIVVCENVADMLSLSEMLAGSLT ATIHATEEDYPQVSQLIPRLEEIAGRLVFNGWPTGVEVGY AMVHGGPYPASTHSASTSVGAEAIHRWLRPVAYQALPESL LPDSLKAENPLEIARAVDGKAA D:  NVFYATNAFTGEALPLAFPVHTEVEVNQAATAAAKVARDF RRLNNSKRASLLRTIASELEARSDDIIARAHLETALPEVR LTGEIARTANQLRLFADVVNSGSYHQAILDTPNPTRAPLP KPDIRRQQIALGPVAVFGASNFPLAFSAAGGDTASALAAG CPVIVKGHTAHPGTSQIVAECIEQALKQEQLPQAIFTLLQ GNQRALGQALVSHPEIKAVGFTGSVGGGRALFNLAHERPE PIPFYGELGAINPTFIFPSAMRAKADLADQFVASMTMGCG QFCTKPGVVFALNTPETQAFIETAQSLIRQQSPSTLLTPG IRDSYQSQVVSRGSDDGIDVTFSQAESPCVASALFVTSSE NWRKHPAWEEEIFGPQSLIVVCENVADMLSLSEMLAGSLT ATIHATEEDYPQVSQLIPRLEEIAGRLVFNGWPTGVEVGY AMVHGGPYPASTHSASTSVGAEAIHRWLRPVAYQALPESL LPDSLKAENPLEIARAVDGKAA Description Functional site 1) chain A residue 253 type sequence E description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTA 2) chain A residue 289 type sequence C description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTA 3) chain A residue 172 type sequence K description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPA 4) chain A residue 175 type sequence T description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPA 5) chain A residue 210 type sequence R description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPA 6) chain A residue 377 type sequence E description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPA 7) chain B residue 253 type sequence E description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTB 8) chain B residue 289 type sequence C description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTB 9) chain B residue 172 type sequence K description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPB 10) chain B residue 175 type sequence T description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPB 11) chain B residue 210 type sequence R description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPB 12) chain B residue 377 type sequence E description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPB 13) chain C residue 253 type sequence E description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTC 14) chain C residue 289 type sequence C description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTC 15) chain C residue 172 type sequence K description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPC 16) chain C residue 175 type sequence T description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPC 17) chain C residue 210 type sequence R description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPC 18) chain C residue 377 type sequence E description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPC 19) chain D residue 253 type sequence E description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTD 20) chain D residue 289 type sequence C description THE KEY RESIDUES AROUND THE ACTIVE SITE source : CTD 21) chain D residue 172 type sequence K description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPD 22) chain D residue 175 type sequence T description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPD 23) chain D residue 210 type sequence R description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPD 24) chain D residue 377 type sequence E description KEY RESIDUES WHICH INTERACT WITH THE NADP COFACTOR source : NPD 25) chain A residue 146 type sequence S description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 26) chain A residue 172 type sequence K description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 27) chain A residue 174 type sequence H description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 28) chain A residue 175 type sequence T description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 29) chain A residue 210 type sequence R description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 30) chain A residue 214 type sequence Q description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 31) chain A residue 227 type sequence F description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 32) chain A residue 229 type sequence G description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 33) chain A residue 230 type sequence S description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 34) chain A residue 233 type sequence G description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 35) chain A residue 237 type sequence L description BINDING SITE FOR RESIDUE NAP A 650 source : AC1 36) chain A residue 6 type sequence D description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 37) chain B residue 146 type sequence S description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 38) chain B residue 172 type sequence K description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 39) chain B residue 174 type sequence H description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 40) chain B residue 175 type sequence T description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 41) chain B residue 210 type sequence R description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 42) chain B residue 214 type sequence Q description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 43) chain B residue 227 type sequence F description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 44) chain B residue 230 type sequence S description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 45) chain B residue 233 type sequence G description BINDING SITE FOR RESIDUE NAP B 750 source : AC2 46) chain C residue 146 type sequence S description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 47) chain C residue 172 type sequence K description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 48) chain C residue 174 type sequence H description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 49) chain C residue 175 type sequence T description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 50) chain C residue 210 type sequence R description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 51) chain C residue 214 type sequence Q description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 52) chain C residue 227 type sequence F description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 53) chain C residue 229 type sequence G description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 54) chain C residue 230 type sequence S description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 55) chain C residue 233 type sequence G description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 56) chain C residue 237 type sequence L description BINDING SITE FOR RESIDUE NAP C 850 source : AC3 57) chain D residue 146 type sequence S description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 58) chain D residue 172 type sequence K description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 59) chain D residue 174 type sequence H description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 60) chain D residue 175 type sequence T description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 61) chain D residue 210 type sequence R description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 62) chain D residue 214 type sequence Q description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 63) chain D residue 227 type sequence F description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 64) chain D residue 230 type sequence S description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 65) chain D residue 233 type sequence G description BINDING SITE FOR RESIDUE NAP D 950 source : AC4 66) chain C residue 253 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 67) chain C residue 289 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 68) chain D residue 253 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 69) chain D residue 289 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 70) chain A residue 253 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 71) chain A residue 289 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 72) chain B residue 253 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 73) chain B residue 289 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 74) chain B residue 229 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 75) chain C residue 229 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 76) chain D residue 229 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 77) chain A residue 229 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2

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