eF-site ID 1cg2-ABCD PDB Code 1cg2 Chain A, B, C, D click to enlarge Title CARBOXYPEPTIDASE G2 Classification METALLOCARBOXYPEPTIDASE Compound CARBOXYPEPTIDASE G2 Source Pseudomonas sp. (strain RS-16) (CBPG_PSES6) Sequence A:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH SDKAEYVDISAIPRRLYMAARLIMDLGAG B:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH SDKAEYVDISAIPRRLYMAARLIMDLGAG C:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH SDKAEYVDISAIPRRLYMAARLIMDLGAG D:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH SDKAEYVDISAIPRRLYMAARLIMDLGAG Description Functional site 1) chain A residue 112 type sequence H description CATALYTIC SITE. source : CTA 2) chain A residue 141 type sequence D description CATALYTIC SITE. source : CTA 3) chain A residue 176 type sequence E description CATALYTIC SITE. source : CTA 4) chain A residue 200 type sequence E description CATALYTIC SITE. source : CTA 5) chain A residue 385 type sequence H description CATALYTIC SITE. source : CTA 6) chain B residue 112 type sequence H description CATALYTIC SITE. source : CTB 7) chain B residue 141 type sequence D description CATALYTIC SITE. source : CTB 8) chain B residue 176 type sequence E description CATALYTIC SITE. source : CTB 9) chain B residue 200 type sequence E description CATALYTIC SITE. source : CTB 10) chain B residue 385 type sequence H description CATALYTIC SITE. source : CTB 11) chain C residue 112 type sequence H description CATALYTIC SITE. source : CTC 12) chain C residue 141 type sequence D description CATALYTIC SITE. source : CTC 13) chain C residue 176 type sequence E description CATALYTIC SITE. source : CTC 14) chain C residue 200 type sequence E description CATALYTIC SITE. source : CTC 15) chain C residue 385 type sequence H description CATALYTIC SITE. source : CTC 16) chain D residue 112 type sequence H description CATALYTIC SITE. source : CTD 17) chain D residue 141 type sequence D description CATALYTIC SITE. source : CTD 18) chain D residue 176 type sequence E description CATALYTIC SITE. source : CTD 19) chain D residue 200 type sequence E description CATALYTIC SITE. source : CTD 20) chain D residue 385 type sequence H description CATALYTIC SITE. source : CTD 21) chain A residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN A 500 source : AC1 22) chain A residue 176 type sequence E description BINDING SITE FOR RESIDUE ZN A 500 source : AC1 23) chain A residue 385 type sequence H description BINDING SITE FOR RESIDUE ZN A 500 source : AC1 24) chain A residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 25) chain A residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 26) chain A residue 175 type sequence E description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 27) chain A residue 200 type sequence E description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 28) chain A residue 229 type sequence H description BINDING SITE FOR RESIDUE ZN A 502 source : AC3 29) chain C residue 387 type sequence D description BINDING SITE FOR RESIDUE ZN A 502 source : AC3 30) chain A residue 256 type sequence D description BINDING SITE FOR RESIDUE ZN A 503 source : AC4 31) chain B residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN B 500 source : AC5 32) chain B residue 176 type sequence E description BINDING SITE FOR RESIDUE ZN B 500 source : AC5 33) chain B residue 385 type sequence H description BINDING SITE FOR RESIDUE ZN B 500 source : AC5 34) chain B residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN B 501 source : AC6 35) chain B residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN B 501 source : AC6 36) chain B residue 175 type sequence E description BINDING SITE FOR RESIDUE ZN B 501 source : AC6 37) chain B residue 200 type sequence E description BINDING SITE FOR RESIDUE ZN B 501 source : AC6 38) chain B residue 229 type sequence H description BINDING SITE FOR RESIDUE ZN B 502 source : AC7 39) chain D residue 387 type sequence D description BINDING SITE FOR RESIDUE ZN B 502 source : AC7 40) chain C residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN C 500 source : AC8 41) chain C residue 176 type sequence E description BINDING SITE FOR RESIDUE ZN C 500 source : AC8 42) chain C residue 385 type sequence H description BINDING SITE FOR RESIDUE ZN C 500 source : AC8 43) chain C residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 44) chain C residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 45) chain C residue 175 type sequence E description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 46) chain C residue 200 type sequence E description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 47) chain A residue 387 type sequence D description BINDING SITE FOR RESIDUE ZN C 502 source : BC1 48) chain C residue 229 type sequence H description BINDING SITE FOR RESIDUE ZN C 502 source : BC1 49) chain D residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN D 500 source : BC2 50) chain D residue 176 type sequence E description BINDING SITE FOR RESIDUE ZN D 500 source : BC2 51) chain D residue 385 type sequence H description BINDING SITE FOR RESIDUE ZN D 500 source : BC2 52) chain D residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN D 501 source : BC3 53) chain D residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN D 501 source : BC3 54) chain D residue 175 type sequence E description BINDING SITE FOR RESIDUE ZN D 501 source : BC3 55) chain D residue 200 type sequence E description BINDING SITE FOR RESIDUE ZN D 501 source : BC3 56) chain B residue 387 type sequence D description BINDING SITE FOR RESIDUE ZN D 502 source : BC4 57) chain D residue 229 type sequence H description BINDING SITE FOR RESIDUE ZN D 502 source : BC4 58) chain A residue 112 type catalytic sequence H description 447 source MCSA : MCSA1 59) chain A residue 141 type catalytic sequence D description 447 source MCSA : MCSA1 60) chain A residue 175 type catalytic sequence E description 447 source MCSA : MCSA1 61) chain A residue 176 type catalytic sequence E description 447 source MCSA : MCSA1 62) chain A residue 200 type catalytic sequence E description 447 source MCSA : MCSA1 63) chain A residue 385 type catalytic sequence H description 447 source MCSA : MCSA1 64) chain B residue 112 type catalytic sequence H description 447 source MCSA : MCSA2 65) chain B residue 141 type catalytic sequence D description 447 source MCSA : MCSA2 66) chain B residue 175 type catalytic sequence E description 447 source MCSA : MCSA2 67) chain B residue 176 type catalytic sequence E description 447 source MCSA : MCSA2 68) chain B residue 200 type catalytic sequence E description 447 source MCSA : MCSA2 69) chain B residue 385 type catalytic sequence H description 447 source MCSA : MCSA2 70) chain C residue 112 type catalytic sequence H description 447 source MCSA : MCSA3 71) chain C residue 141 type catalytic sequence D description 447 source MCSA : MCSA3 72) chain C residue 175 type catalytic sequence E description 447 source MCSA : MCSA3 73) chain C residue 176 type catalytic sequence E description 447 source MCSA : MCSA3 74) chain C residue 200 type catalytic sequence E description 447 source MCSA : MCSA3 75) chain C residue 385 type catalytic sequence H description 447 source MCSA : MCSA3 76) chain D residue 112 type catalytic sequence H description 447 source MCSA : MCSA4 77) chain D residue 141 type catalytic sequence D description 447 source MCSA : MCSA4 78) chain D residue 175 type catalytic sequence E description 447 source MCSA : MCSA4 79) chain D residue 176 type catalytic sequence E description 447 source MCSA : MCSA4 80) chain D residue 200 type catalytic sequence E description 447 source MCSA : MCSA4 81) chain D residue 385 type catalytic sequence H description 447 source MCSA : MCSA4 82) chain A residue 107-116 type prosite sequence LLLMSHMDTV description ARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. LLLMSHmDTV source prosite : PS00758 83) chain A residue 139-178 type prosite sequence IADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKG description ARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. IADdKGgnAviLhtlkllkeygvrdygt.ItVLFntDEEkG source prosite : PS00759 84) chain A residue 114 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 85) chain B residue 114 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 86) chain C residue 114 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 87) chain D residue 114 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 88) chain A residue 175 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI2 89) chain B residue 175 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI2 90) chain C residue 175 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI2 91) chain D residue 175 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI2 92) chain A residue 112 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 93) chain B residue 385 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 94) chain C residue 112 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 95) chain C residue 141 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 96) chain C residue 176 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 97) chain C residue 200 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 98) chain C residue 385 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 99) chain D residue 112 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 100) chain D residue 141 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 101) chain D residue 176 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 102) chain D residue 200 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 103) chain A residue 141 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 104) chain D residue 385 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 105) chain A residue 176 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 106) chain A residue 200 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 107) chain A residue 385 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 108) chain B residue 112 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 109) chain B residue 141 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 110) chain B residue 176 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 111) chain B residue 200 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3

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