eF-site ID 1s07-A PDB Code 1s07 Chain A click to enlarge Title Crystal Structure of the R253A Mutant of 7,8-Diaminopelargonic Acid Synthase Classification TRANSFERASE Compound Adenosylmethionine-8-amino-7-oxononanoate aminotransferase Source Escherichia coli (strain K12) (BIOA_ECOLI) Sequence A:  MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILS DGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMF GGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGI LLIADEIATGFGATGKLFACEHAEIAPDILCLGKALTGGT MTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAA NASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVR VLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM PPYIILPQQLQRLTAAVNRAVQDETFFCQ Description Functional site 1) chain A residue 96 type sequence V description BINDING SITE FOR RESIDUE NA A 501 source : AC1 2) chain A residue 99 type sequence T description BINDING SITE FOR RESIDUE NA A 501 source : AC1 3) chain A residue 100 type sequence P description BINDING SITE FOR RESIDUE NA A 501 source : AC1 4) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE NA A 501 source : AC1 5) chain A residue 113 type sequence S description BINDING SITE FOR RESIDUE PLP A 430 source : AC3 6) chain A residue 144 type sequence Y description BINDING SITE FOR RESIDUE PLP A 430 source : AC3 7) chain A residue 145 type sequence H description BINDING SITE FOR RESIDUE PLP A 430 source : AC3 8) chain A residue 211 type sequence E description BINDING SITE FOR RESIDUE PLP A 430 source : AC3 9) chain A residue 245 type sequence D description BINDING SITE FOR RESIDUE PLP A 430 source : AC3 10) chain A residue 248 type sequence A description BINDING SITE FOR RESIDUE PLP A 430 source : AC3 11) chain A residue 274 type sequence K description BINDING SITE FOR RESIDUE PLP A 430 source : AC3 12) chain A residue 308 type sequence P description BINDING SITE FOR RESIDUE PLP B 431 source : AC4 13) chain A residue 309 type sequence T description BINDING SITE FOR RESIDUE PLP B 431 source : AC4 14) chain A residue 17 type sequence Y description BINDING SITE FOR RESIDUE IPA B 600 source : AC5 15) chain A residue 17 type catalytic sequence Y description 249 source MCSA : MCSA1 16) chain A residue 144 type catalytic sequence Y description 249 source MCSA : MCSA1 17) chain A residue 245 type catalytic sequence D description 249 source MCSA : MCSA1 18) chain A residue 274 type catalytic sequence K description 249 source MCSA : MCSA1 19) 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 20) 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 21) 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 22) 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 23) chain A residue 144 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 24) 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 25) chain A residue 242-279 type prosite sequence LIADEIATGFGATGKLFACEHAEIAPDILCLGKALTGG description AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEIat.GFgAtGklfacehaeiap....DILclGKaltGG source prosite : PS00600 26) 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 27) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 28) 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 29) 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

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