eF-site ID 1mly-A PDB Code 1mly Chain A 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 A:  MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILS DGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMF GGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMGEWDERDMVGFARLMAAH RHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGIL LIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTM TLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAAN ASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVRV LGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMP PYIILPQQLQRLTAAVNRAVQDETFFC 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 A residue 96 type sequence V description BINDING SITE FOR RESIDUE NA A 702 source : AC4 9) chain A residue 99 type sequence T description BINDING SITE FOR RESIDUE NA A 702 source : AC4 10) chain A residue 100 type sequence P description BINDING SITE FOR RESIDUE NA A 702 source : AC4 11) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE NA A 702 source : AC4 12) chain A residue 112 type sequence G description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 13) chain A residue 113 type sequence S description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 14) chain A residue 144 type sequence Y description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 15) chain A residue 145 type sequence H description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 16) chain A residue 146 type sequence G description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 17) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 18) chain A residue 245 type sequence D description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 19) chain A residue 247 type sequence I description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 20) chain A residue 274 type sequence K description BINDING SITE FOR RESIDUE PLP A 730 source : AC5 21) chain A residue 308 type sequence P description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 22) chain A residue 309 type sequence T description BINDING SITE FOR RESIDUE PLP B 830 source : AC6 23) 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 24) 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 25) chain A residue 17 type catalytic sequence Y description 249 source MCSA : MCSA1 26) chain A residue 144 type catalytic sequence Y description 249 source MCSA : MCSA1 27) chain A residue 245 type catalytic sequence D description 249 source MCSA : MCSA1 28) chain A residue 274 type catalytic sequence K description 249 source MCSA : MCSA1 29) 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 30) 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 31) 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 32) 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 33) chain A residue 144 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 34) 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 35) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 36) 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 37) 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

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