eF-site ID 1cg2-C PDB Code 1cg2 Chain C click to enlarge Title CARBOXYPEPTIDASE G2 Classification METALLOCARBOXYPEPTIDASE Compound CARBOXYPEPTIDASE G2 Source Pseudomonas sp. (strain RS-16) (CBPG_PSES6) Sequence C:  QKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAA AGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGK NLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGG NAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDL IQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITG KASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNW TIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEER AQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYK EAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYH SDKAEYVDISAIPRRLYMAARLIMDLGAG Description Functional site 1) chain C residue 112 type sequence H description CATALYTIC SITE. source : CTC 2) chain C residue 141 type sequence D description CATALYTIC SITE. source : CTC 3) chain C residue 176 type sequence E description CATALYTIC SITE. source : CTC 4) chain C residue 200 type sequence E description CATALYTIC SITE. source : CTC 5) chain C residue 385 type sequence H description CATALYTIC SITE. source : CTC 6) chain C residue 387 type sequence D description BINDING SITE FOR RESIDUE ZN A 502 source : AC3 7) chain C residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN C 500 source : AC8 8) chain C residue 176 type sequence E description BINDING SITE FOR RESIDUE ZN C 500 source : AC8 9) chain C residue 385 type sequence H description BINDING SITE FOR RESIDUE ZN C 500 source : AC8 10) chain C residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 11) chain C residue 141 type sequence D description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 12) chain C residue 175 type sequence E description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 13) chain C residue 200 type sequence E description BINDING SITE FOR RESIDUE ZN C 501 source : AC9 14) chain C residue 229 type sequence H description BINDING SITE FOR RESIDUE ZN C 502 source : BC1 15) chain C residue 114 type ACT_SITE sequence D description ACT_SITE => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 112 type catalytic sequence H description 447 source MCSA : MCSA3 17) chain C residue 141 type catalytic sequence D description 447 source MCSA : MCSA3 18) chain C residue 175 type catalytic sequence E description 447 source MCSA : MCSA3 19) chain C residue 176 type catalytic sequence E description 447 source MCSA : MCSA3 20) chain C residue 200 type catalytic sequence E description 447 source MCSA : MCSA3 21) chain C residue 385 type catalytic sequence H description 447 source MCSA : MCSA3 22) chain C residue 175 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 112 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 24) chain C residue 141 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 25) chain C residue 176 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 26) chain C residue 200 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3 27) chain C residue 385 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9083113 source Swiss-Prot : SWS_FT_FI3

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