eF-site ID 5i63-ABCD PDB Code 5i63 Chain A, B, C, D click to enlarge Title Crystal structure of TEM1 beta-lactamase mutant I263N in the presence of 1.2 MPa xenon Classification HYDROLASE Compound Beta-lactamase TEM Source (BLAT_ECOLX) Sequence A:  HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEER FPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEY SPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP KELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTTPAA MATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVNYTTG SQATMDERNRQIAEIGASLIKHW B:  HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEER FPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEY SPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP KELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTTPAA MATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVNYTTG SQATMDERNRQIAEIGASLIKHW C:  HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEER FPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEY SPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP KELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTTPAA MATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVNYTTG SQATMDERNRQIAEIGASLIKHW D:  HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEER FPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEY SPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP KELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTTPAA MATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSAL PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVNYTTG SQATMDERNRQIAEIGASLIKHW Description Functional site 1) chain A residue 40 type sequence L description binding site for residue XE A 301 source : AC1 2) chain A residue 265 type sequence T description binding site for residue XE A 301 source : AC1 3) chain A residue 263 type sequence N description binding site for residue XE A 302 source : AC2 4) chain A residue 279 type sequence I description binding site for residue XE A 302 source : AC2 5) chain A residue 282 type sequence I description binding site for residue XE A 302 source : AC2 6) chain B residue 263 type sequence N description binding site for residue XE B 301 source : AC3 7) chain B residue 279 type sequence I description binding site for residue XE B 301 source : AC3 8) chain B residue 221 type sequence L description binding site for residue XE B 302 source : AC4 9) chain B residue 279 type sequence I description binding site for residue XE B 302 source : AC4 10) chain C residue 221 type sequence L description binding site for residue XE C 302 source : AC5 11) chain D residue 263 type sequence N description binding site for residue XE D 301 source : AC6 12) chain D residue 279 type sequence I description binding site for residue XE D 301 source : AC6 13) chain D residue 282 type sequence I description binding site for residue XE D 301 source : AC6 14) chain D residue 221 type sequence L description binding site for residue XE D 302 source : AC7 15) chain A residue 70 type catalytic sequence S description 2 source MCSA : MCSA1 16) chain A residue 73 type catalytic sequence K description 2 source MCSA : MCSA1 17) chain A residue 130 type catalytic sequence S description 2 source MCSA : MCSA1 18) chain A residue 166 type catalytic sequence E description 2 source MCSA : MCSA1 19) chain A residue 234 type catalytic sequence K description 2 source MCSA : MCSA1 20) chain A residue 237 type catalytic sequence A description 2 source MCSA : MCSA1 21) chain B residue 70 type catalytic sequence S description 2 source MCSA : MCSA2 22) chain B residue 73 type catalytic sequence K description 2 source MCSA : MCSA2 23) chain B residue 130 type catalytic sequence S description 2 source MCSA : MCSA2 24) chain B residue 166 type catalytic sequence E description 2 source MCSA : MCSA2 25) chain B residue 234 type catalytic sequence K description 2 source MCSA : MCSA2 26) chain B residue 237 type catalytic sequence A description 2 source MCSA : MCSA2 27) chain C residue 70 type catalytic sequence S description 2 source MCSA : MCSA3 28) chain C residue 73 type catalytic sequence K description 2 source MCSA : MCSA3 29) chain C residue 130 type catalytic sequence S description 2 source MCSA : MCSA3 30) chain C residue 166 type catalytic sequence E description 2 source MCSA : MCSA3 31) chain C residue 234 type catalytic sequence K description 2 source MCSA : MCSA3 32) chain C residue 237 type catalytic sequence A description 2 source MCSA : MCSA3 33) chain D residue 70 type catalytic sequence S description 2 source MCSA : MCSA4 34) chain D residue 73 type catalytic sequence K description 2 source MCSA : MCSA4 35) chain D residue 130 type catalytic sequence S description 2 source MCSA : MCSA4 36) chain D residue 166 type catalytic sequence E description 2 source MCSA : MCSA4 37) chain D residue 234 type catalytic sequence K description 2 source MCSA : MCSA4 38) chain D residue 237 type catalytic sequence A description 2 source MCSA : MCSA4 39) chain A residue 66-81 type prosite sequence FPMMSTFKVLLCGAVL description BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL source prosite : PS00146 40) chain A residue 70 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 41) chain B residue 70 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 42) chain C residue 70 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 43) chain D residue 70 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 44) chain A residue 168 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 45) chain B residue 168 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 46) chain C residue 168 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 47) chain D residue 168 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI2 48) chain A residue 234 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 49) chain B residue 234 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 50) chain C residue 234 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 51) chain D residue 234 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3

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