eF-site ID 1a2z-ABCD PDB Code 1a2z Chain A, B, C, D click to enlarge Title PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS Classification PEPTIDASE Compound PYRROLIDONE CARBOXYL PEPTIDASE Source Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) (PCP_THELI) Sequence A:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL AVKVSLDYLEKDRDDIKIPL B:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL AVKVSLDYLEKDRDDIKIPL C:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL AVKVSLDYLEKDRDDIKIPL D:  MKKVLITGFEPFGGDSKNPTEQIAKYFDRKQIGNAMVYGR VLPVSVKRATIELKRYLEEIKPEIVINLGLAPTYSNITVE RIAVNIIDARIPDNDGYQPIDEKIEEDAPLAYMATLPVRA ITKTLRDNGIPATISYSAGTYLCNYVMFKTLHFSKIEGYP LKAGFIHVPYTPDQVVNKFFLLGKNTPSMCLEAEIKAIEL AVKVSLDYLEKDRDDIKIPL Description (1)  PYRROLIDONE CARBOXYL PEPTIDASE Functional site 1) chain A residue 80 type sequence E description CATALYTIC TRIAD. source : AVE 2) chain A residue 143 type sequence C description CATALYTIC TRIAD. source : AVE 3) chain A residue 167 type sequence H description CATALYTIC TRIAD. source : AVE 4) chain A residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 A 621 source : AC1 5) chain B residue 38 type sequence Y description BINDING SITE FOR RESIDUE SO4 A 621 source : AC1 6) chain B residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 B 622 source : AC2 7) chain B residue 2 type sequence K description BINDING SITE FOR RESIDUE SO4 B 622 source : AC2 8) chain B residue 34 type sequence N description BINDING SITE FOR RESIDUE SO4 B 622 source : AC2 9) chain C residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 C 623 source : AC3 10) chain C residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 D 624 source : AC4 11) chain D residue 1 type sequence M description BINDING SITE FOR RESIDUE SO4 D 624 source : AC4 12) chain D residue 2 type sequence K description BINDING SITE FOR RESIDUE SO4 D 624 source : AC4 13) chain D residue 34 type sequence N description BINDING SITE FOR RESIDUE SO4 D 624 source : AC4 14) chain A residue 69-85 type prosite sequence GLAPTYSNITVERIAVN description PYRASE_GLU Pyrrolidone-carboxylate peptidase glutamic acid active site. GlaPtysnITvERIAvN source prosite : PS01333 15) chain A residue 130-144 type prosite sequence IPATISYSAGTYLCN description PYRASE_CYS Pyrrolidone-carboxylate peptidase cysteine active site. IpAtISySAGtYLCN source prosite : PS01334 16) chain A residue 80 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 17) chain D residue 80 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 18) chain D residue 143 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 19) chain D residue 167 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 20) chain A residue 143 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 21) chain A residue 167 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 22) chain B residue 80 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 23) chain B residue 143 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 24) chain B residue 167 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1 25) chain C residue 80 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 26) chain C residue 143 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 27) chain C residue 167 type ACT_SITE sequence H description source Swiss-Prot : SWS_FT_FI1

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