eF-site ID 1s09-AB PDB Code 1s09 Chain A, B click to enlarge Title Crystal Structure of the Y144F 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 KMALQYWQAKGEARQRFLTFRNGFHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMGEWDERDMVGFARLMAAH RHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGIL LIADEIATGFGRTGKLFACEHAEIAPDILCLGXALTGGTM TLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAAN ASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVRV LGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLMP PYIILPQQLQRLTAAVNRAVQDETFFC B:  MTTDDLAFDQRHILHPYTSMTSPLPVYPVVSAEGCELILS DGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMF GGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGFHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGI LLIADEIATGFGRTGKLFACEHAEIAPDILCLGXALTGGT MTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAA NASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVR VLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM PPYIILPQQLQRLTAAVNRAVQDETFFC Description Functional site 1) chain A residue 96 type sequence V description BINDING SITE FOR RESIDUE NA A 1501 source : AC1 2) chain A residue 99 type sequence T description BINDING SITE FOR RESIDUE NA A 1501 source : AC1 3) chain A residue 100 type sequence P description BINDING SITE FOR RESIDUE NA A 1501 source : AC1 4) chain A residue 103 type sequence L description BINDING SITE FOR RESIDUE NA A 1501 source : AC1 5) chain B residue 96 type sequence V description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 6) chain B residue 99 type sequence T description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 7) chain B residue 100 type sequence P description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 8) chain B residue 103 type sequence L description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 9) chain A residue 17 type catalytic sequence Y description 249 source MCSA : MCSA1 10) chain A residue 144 type catalytic sequence F description 249 source MCSA : MCSA1 11) chain A residue 245 type catalytic sequence D description 249 source MCSA : MCSA1 12) chain A residue 274 type catalytic sequence X description 249 source MCSA : MCSA1 13) chain B residue 17 type catalytic sequence Y description 249 source MCSA : MCSA2 14) chain B residue 144 type catalytic sequence F description 249 source MCSA : MCSA2 15) chain B residue 245 type catalytic sequence D description 249 source MCSA : MCSA2 16) chain B residue 274 type catalytic sequence X description 249 source MCSA : MCSA2 17) 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 18) chain A residue 274 type BINDING sequence X description BINDING => ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:12218056, ECO:0007744|PDB:1MLY, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI1 19) 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 20) chain B residue 274 type BINDING sequence X 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 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 24) 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 25) chain A residue 144 type BINDING sequence F description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 144 type BINDING sequence F description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 27) 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 28) 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 29) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 31) 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 32) 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 33) 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 34) 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 35) chain A residue 242-279 type prosite sequence LIADEIATGFGRTGKLFACEHAEIAPDILCLGXALTGG description AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEIat.GFgRtGklfacehaeiap....DILclGKaltGG source prosite : PS00600 36) chain A residue 274 type MOD_RES sequence X 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 37) chain B residue 274 type MOD_RES sequence X 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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