eF-site ID 1mly-AB PDB Code 1mly Chain A, B click to enlarge Title Crystal Structure of 7,8-Diaminopelargonic Acid Synthase in complex with the cis isomer of amiclenomycin Classification TRANSFERASE Compound 7,8-diamino-pelargonic acid aminotransferase Source Escherichia coli (strain K12) (BIOA_ECOLI) Sequence A:  MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILS DGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMF GGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMGEWDERDMVGFARLMAAH RHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGIL LIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTM TLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAAN ASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVRV LGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMP PYIILPQQLQRLTAAVNRAVQDETFFC B:  MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILS DGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMF GGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGI LLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGT MTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAA NASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVR VLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM PPYIILPQQLQRLTAAVNRAVQDETFFC Description Functional site 1) chain A residue 52 type sequence W description BINDING SITE FOR RESIDUE ACZ A 731 source : AC1 2) chain A residue 53 type sequence W description BINDING SITE FOR RESIDUE ACZ A 731 source : AC1 3) chain A residue 144 type sequence Y description BINDING SITE FOR RESIDUE ACZ A 731 source : AC1 4) chain A residue 274 type sequence K description BINDING SITE FOR RESIDUE ACZ A 731 source : AC1 5) chain A residue 391 type sequence R description BINDING SITE FOR RESIDUE ACZ A 731 source : AC1 6) chain A residue 393 type sequence F description BINDING SITE FOR RESIDUE ACZ A 731 source : AC1 7) chain A residue 309 type sequence T description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 8) chain B residue 52 type sequence W description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 9) chain B residue 144 type sequence Y description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 10) chain B residue 217 type sequence A description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 11) chain B residue 391 type sequence R description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 12) chain B residue 393 type sequence F description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 13) chain B residue 398 type sequence Y description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 14) chain B residue 96 type sequence V description BINDING SITE FOR RESIDUE NA B 701 source : AC3 15) chain B residue 99 type sequence T description BINDING SITE FOR RESIDUE NA B 701 source : AC3 16) chain B residue 100 type sequence P description BINDING SITE FOR RESIDUE NA B 701 source : AC3 17) chain B residue 103 type sequence L description BINDING SITE FOR RESIDUE NA B 701 source : AC3 18) chain A residue 96 type sequence V description BINDING SITE FOR RESIDUE NA A 702 source : AC4 19) chain A residue 99 type sequence T description BINDING SITE FOR RESIDUE NA A 702 source : AC4 20) chain A residue 100 type sequence P description BINDING SITE FOR RESIDUE NA A 702 source : AC4 21) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE NA A 702 source : AC4 22) chain A residue 112 type sequence G description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 23) chain A residue 113 type sequence S description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 24) chain A residue 144 type sequence Y description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 25) chain A residue 145 type sequence H description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 26) chain A residue 146 type sequence G description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 27) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 28) chain A residue 245 type sequence D description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 29) chain A residue 247 type sequence I description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 30) chain A residue 274 type sequence K description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 31) chain B residue 308 type sequence P description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 32) chain B residue 309 type sequence T description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 33) chain A residue 308 type sequence P description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 34) chain A residue 309 type sequence T description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 35) chain B residue 53 type sequence W description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 36) chain B residue 112 type sequence G description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 37) chain B residue 113 type sequence S description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 38) chain B residue 145 type sequence H description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 39) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 40) chain B residue 245 type sequence D description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 41) chain B residue 247 type sequence I description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 42) chain B residue 248 type sequence A description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 43) chain B residue 274 type sequence K description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 44) chain A residue 17 type catalytic sequence Y description 249 source MCSA : MCSA1 45) chain A residue 144 type catalytic sequence Y description 249 source MCSA : MCSA1 46) chain A residue 245 type catalytic sequence D description 249 source MCSA : MCSA1 47) chain A residue 274 type catalytic sequence K description 249 source MCSA : MCSA1 48) chain B residue 17 type catalytic sequence Y description 249 source MCSA : MCSA2 49) chain B residue 144 type catalytic sequence Y description 249 source MCSA : MCSA2 50) chain B residue 245 type catalytic sequence D description 249 source MCSA : MCSA2 51) chain B residue 274 type catalytic sequence K description 249 source MCSA : MCSA2 52) chain A residue 52 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 274 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 52 type BINDING sequence W description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 274 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 57) chain B residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 58) chain A residue 391 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY, ECO:0007744|PDB:1MLZ, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI6 59) chain B residue 391 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY, ECO:0007744|PDB:1MLZ, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI6 60) chain A residue 17 type SITE sequence Y description Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000305 source Swiss-Prot : SWS_FT_FI7 61) chain B residue 17 type SITE sequence Y description Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000305 source Swiss-Prot : SWS_FT_FI7 62) chain A residue 242-279 type prosite sequence LIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGG description AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEIat.GFgRtGklfacehaeiap....DILclGKaltGG source prosite : PS00600 63) chain A residue 112 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S07 source Swiss-Prot : SWS_FT_FI2 64) chain A residue 308 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S07 source Swiss-Prot : SWS_FT_FI2 65) chain B residue 112 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S07 source Swiss-Prot : SWS_FT_FI2 66) chain B residue 308 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S07 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 274 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S06, ECO:0007744|PDB:1S08, ECO:0007744|PDB:1S09, ECO:0007744|PDB:1S0A source Swiss-Prot : SWS_FT_FI8 68) chain B residue 274 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1DTY, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S06, ECO:0007744|PDB:1S08, ECO:0007744|PDB:1S09, ECO:0007744|PDB:1S0A source Swiss-Prot : SWS_FT_FI8 69) chain A residue 144 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 70) chain B residue 144 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 71) chain A residue 245 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S07 source Swiss-Prot : SWS_FT_FI4 72) chain B residue 245 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557, ECO:0007744|PDB:1MGV, ECO:0007744|PDB:1QJ3, ECO:0007744|PDB:1QJ5, ECO:0007744|PDB:1S07 source Swiss-Prot : SWS_FT_FI4

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