eF-site ID 1cg2-A PDB Code 1cg2 Chain A 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 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 A residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN A 500 source : AC1 7) chain A residue 176 type sequence E description BINDING SITE FOR RESIDUE ZN A 500 source : AC1 8) chain A residue 385 type sequence H description BINDING SITE FOR RESIDUE ZN A 500 source : AC1 9) chain A residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 10) chain A residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 11) chain A residue 175 type sequence E description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 12) chain A residue 200 type sequence E description BINDING SITE FOR RESIDUE ZN A 501 source : AC2 13) chain A residue 229 type sequence H description BINDING SITE FOR RESIDUE ZN A 502 source : AC3 14) chain A residue 256 type sequence D description BINDING SITE FOR RESIDUE ZN A 503 source : AC4 15) chain A residue 387 type sequence D description BINDING SITE FOR RESIDUE ZN C 502 source : BC1 16) chain A residue 114 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 112 type catalytic sequence H description 447 source MCSA : MCSA1 18) chain A residue 141 type catalytic sequence D description 447 source MCSA : MCSA1 19) chain A residue 175 type catalytic sequence E description 447 source MCSA : MCSA1 20) chain A residue 176 type catalytic sequence E description 447 source MCSA : MCSA1 21) chain A residue 200 type catalytic sequence E description 447 source MCSA : MCSA1 22) chain A residue 385 type catalytic sequence H description 447 source MCSA : MCSA1 23) chain A residue 175 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI2 24) 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 25) 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 26) chain A residue 112 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 141 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 176 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 200 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 385 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3

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