eF-site ID 2wld-ABC PDB Code 2wld Chain A, B, C click to enlarge Title Crystallographic analysis of the polysialic acid O-acetyltransferase OatWY Classification TRANSFERASE Compound POLYSIALIC ACID O-ACETYLTRANSFERASE Source Neisseria meningitidis (Q93S40_NEIME) Sequence A:  MYSEQGINNTINISTTSLTNATQLTVIGNNNSVYIGNNCK IVSSNIRLKGNNITLFIADDVEIMGLVCSLHSDCSLQIQA KTTMGNGEITIAEKGKISIGKDCMLAHGYEIRNTDMHPIY SLENGERINHGKDVIIGNHVWLGRNVTILKGVCIPNNVVV GSHTVLYKSFKEPNCVIAGSPAKIVKENIVWGRKMYHSTM YDDPTLNEFY B:  MYSEQGINNTINISTTSLTNATQLTVIGNNNSVYIGNNCK IVSSNIRLKGNNITLFIADDVEIMGLVCSLHSDCSLQIQA KTTMGNGEITIAEKGKISIGKDCMLAHGYEIRNTDMHPIY SLENGERINHGKDVIIGNHVWLGRNVTILKGVCIPNNVVV GSHTVLYKSFKEPNCVIAGSPAKIVKENIVWGRKMYHSTM YDDPTLNEFYK C:  MYSEQGINNTINISTTSLTNATQLTVIGNNNSVYIGNNCK IVSSNIRLKGNNITLFIADDVEIMGLVCSLHSDCSLQIQA KTTMGNGEITIAEKGKISIGKDCMLAHGYEIRNTDMHPIY SLENGERINHGKDVIIGNHVWLGRNVTILKGVCIPNNVVV GSHTVLYKSFKEPNCVIAGSPAKIVKENIVWGRKMYHSTM YDDPTLNEFYK Description Functional site 1) chain C residue 119 type sequence D description BINDING SITE FOR RESIDUE ACT C 1216 source : AC1 2) chain C residue 154 type sequence K description BINDING SITE FOR RESIDUE ACT C 1216 source : AC1 3) chain A residue 36 type sequence S description BINDING SITE FOR RESIDUE ACT A 1215 source : AC2 4) chain A residue 59 type sequence L description BINDING SITE FOR RESIDUE ACT A 1215 source : AC2 5) chain A residue 60 type sequence F description BINDING SITE FOR RESIDUE ACT A 1215 source : AC2 6) chain A residue 81 type sequence Q description BINDING SITE FOR RESIDUE ACT A 1215 source : AC2 7) chain A residue 83 type sequence Q description BINDING SITE FOR RESIDUE ACT A 1215 source : AC2 8) chain A residue 147 type sequence G description BINDING SITE FOR RESIDUE EDO A 1216 source : AC3 9) chain A residue 69 type sequence G description BINDING SITE FOR RESIDUE EDO A 1217 source : AC4 10) chain A residue 71 type sequence V description BINDING SITE FOR RESIDUE EDO A 1217 source : AC4 11) chain A residue 90 type sequence N description BINDING SITE FOR RESIDUE EDO A 1217 source : AC4 12) chain B residue 75 type sequence H description BINDING SITE FOR RESIDUE EDO B 1216 source : AC5 13) chain B residue 96 type sequence A description BINDING SITE FOR RESIDUE EDO B 1216 source : AC5 14) chain B residue 97 type sequence E description BINDING SITE FOR RESIDUE EDO B 1216 source : AC5 15) chain A residue 8 type sequence E description BINDING SITE FOR RESIDUE EDO A 1218 source : AC6 16) chain A residue 13 type sequence N description BINDING SITE FOR RESIDUE EDO A 1218 source : AC6 17) chain A residue 14 type sequence T description BINDING SITE FOR RESIDUE EDO A 1218 source : AC6 18) chain A residue 15 type sequence I description BINDING SITE FOR RESIDUE EDO A 1218 source : AC6 19) chain A residue 75 type sequence H description BINDING SITE FOR RESIDUE EDO A 1219 source : AC7 20) chain A residue 97 type sequence E description BINDING SITE FOR RESIDUE EDO A 1219 source : AC7 21) chain C residue 147 type sequence G description BINDING SITE FOR RESIDUE EDO C 1217 source : AC8 22) chain A residue 119 type sequence D description BINDING SITE FOR RESIDUE EDO A 1220 source : AC9 23) chain A residue 133 type sequence N description BINDING SITE FOR RESIDUE EDO A 1220 source : AC9 24) chain A residue 154 type sequence K description BINDING SITE FOR RESIDUE EDO A 1220 source : AC9 25) chain A residue 119 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 166 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 190 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 29) chain C residue 119 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 30) chain C residue 148 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 154 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 32) chain C residue 166 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 34) chain C residue 190 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 148 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 154 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 166 type BINDING sequence S description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 171 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 190 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 119 type BINDING sequence D description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 148 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 154 type BINDING sequence K description BINDING => ECO:0000269|PubMed:19525232 source Swiss-Prot : SWS_FT_FI1

Display surface Download Links