eF-site ID 4olg-B PDB Code 4olg Chain B click to enlarge Title Crystal structure of AmpC beta-lactamase in complex with covalently bound N-formyl 7-aminocephalosporanic acid Classification HYDROLASE Compound Beta-lactamase Source Escherichia coli (strain K12) (AMPC_ECOLI) Sequence B:  APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTW GYADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEI KLSDPTTKYWPELTAKQWNGITLLHLATYTAGGLPLQVPD EVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAV KPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDI NEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSI INGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFG SYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNALQ Description (1)  Beta-lactamase (E.C.3.5.2.6) Functional site 1) chain B residue 290 type sequence K description BINDING SITE FOR RESIDUE PO4 A 402 source : AC2 2) chain B residue 64 type sequence S description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 3) chain B residue 119 type sequence L description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 4) chain B residue 150 type sequence Y description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 5) chain B residue 289 type sequence N description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 6) chain B residue 293 type sequence L description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 7) chain B residue 317 type sequence G description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 8) chain B residue 318 type sequence A description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 9) chain B residue 346 type sequence N description BINDING SITE FOR RESIDUE 2TV B 401 source : AC3 10) chain B residue 64 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x source Swiss-Prot : SWS_FT_FI1 11) chain B residue 64 type BINDING sequence S description BINDING => ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:2FFY source Swiss-Prot : SWS_FT_FI2 12) chain B residue 120 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 150 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY source Swiss-Prot : SWS_FT_FI4 14) chain B residue 152 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY source Swiss-Prot : SWS_FT_FI5 15) chain B residue 318 type BINDING sequence A description BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY source Swiss-Prot : SWS_FT_FI5 16) chain B residue 343 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM source Swiss-Prot : SWS_FT_FI6

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