eF-site ID 1mly-B PDB Code 1mly Chain 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 null (BIOA_ECOLI) Sequence B:  MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILS DGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMF GGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGI LLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGT MTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAA NASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVR VLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM PPYIILPQQLQRLTAAVNRAVQDETFFC Description Functional site 1) chain B residue 52 type sequence W description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 2) chain B residue 144 type sequence Y description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 3) chain B residue 217 type sequence A description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 4) chain B residue 391 type sequence R description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 5) chain B residue 393 type sequence F description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 6) chain B residue 398 type sequence Y description BINDING SITE FOR RESIDUE ACZ B 831 source : AC2 7) chain B residue 96 type sequence V description BINDING SITE FOR RESIDUE NA B 701 source : AC3 8) chain B residue 99 type sequence T description BINDING SITE FOR RESIDUE NA B 701 source : AC3 9) chain B residue 100 type sequence P description BINDING SITE FOR RESIDUE NA B 701 source : AC3 10) chain B residue 103 type sequence L description BINDING SITE FOR RESIDUE NA B 701 source : AC3 11) chain B residue 308 type sequence P description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 12) chain B residue 309 type sequence T description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 13) chain B residue 53 type sequence W description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 14) chain B residue 112 type sequence G description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 15) chain B residue 113 type sequence S description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 16) chain B residue 145 type sequence H description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 17) chain B residue 211 type sequence E description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 18) chain B residue 245 type sequence D description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 19) chain B residue 247 type sequence I description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 20) chain B residue 248 type sequence A description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 21) chain B residue 274 type sequence K description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 22) 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 23) 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 24) chain B residue 17 type catalytic sequence Y description 249 source MCSA : MCSA2 25) chain B residue 144 type catalytic sequence Y description 249 source MCSA : MCSA2 26) chain B residue 245 type catalytic sequence D description 249 source MCSA : MCSA2 27) chain B residue 274 type catalytic sequence K description 249 source MCSA : MCSA2 28) 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 29) 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 30) 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 31) 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 32) chain B residue 144 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 33) 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 34) chain B residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 35) 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

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