eF-site ID 1s0a-B PDB Code 1s0a Chain B click to enlarge Title Crystal Structure of the Y17F Mutant of 7,8-Diaminopelargonic Acid Synthase Classification TRANSFERASE Compound Adenosylmethionine-8-amino-7-oxononanoate aminotransferase Source null (BIOA_ECOLI) Sequence B:  MTTDDLAFDQRHILHPFTSMTSPLPVYPVVSAEGCELILS DGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMF GGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAM KMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNS MHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAA HRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGI LLIADEIATGFGRTGKLFACEHAEIAPDILCLGXALTGGT MTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAA NASLAILESGDWQQQVADIEVQLREQLAPARDAEMVADVR VLGAIGVVETTHPVNMAALQKFFVEQGVWIRPFGKLIYLM PPYIILPQQLQRLTAAVNRAVQDETFFC Description Functional site 1) chain B residue 96 type sequence V description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 2) chain B residue 99 type sequence T description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 3) chain B residue 100 type sequence P description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 4) chain B residue 103 type sequence L description BINDING SITE FOR RESIDUE NA B 1502 source : AC2 5) 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 6) 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 7) 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 8) 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 9) chain B residue 144 type BINDING sequence Y description BINDING => ECO:0000305|PubMed:10452893 source Swiss-Prot : SWS_FT_FI3 10) 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 11) chain B residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10452893, ECO:0007744|PDB:1QJ3 source Swiss-Prot : SWS_FT_FI5 12) chain B residue 17 type catalytic sequence F description 249 source MCSA : MCSA2 13) chain B residue 144 type catalytic sequence Y description 249 source MCSA : MCSA2 14) chain B residue 245 type catalytic sequence D description 249 source MCSA : MCSA2 15) chain B residue 274 type catalytic sequence X description 249 source MCSA : MCSA2 16) 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 17) 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 18) chain B residue 17 type SITE sequence F 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

Display surface Download Links