eF-site ID 1xgm-AB PDB Code 1xgm Chain A, B click to enlarge Title METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS Classification AMINOPEPTIDASE Compound METHIONINE AMINOPEPTIDASE Source ORGANISM_SCIENTIFIC: Pyrococcus furiosus; Sequence A:  MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKM IMELGGKPAFPVNLSINEIAAHYTPYKGDTTVLKEGDYLK IDVGVHIDGFIADTAVTVRVGMEEDELMEAAKEALNAAIS VARAGVEIKELGKAIENEIRKRGFKPIVNLSGHKIERYKL HAGISIPNIYRPHDNYVLKEGDVFAIEPFATIGAGQVIEV PPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWL QNDMPEGQLKLALKTLEKAGAIYGYPVLKEIRNGIVAQFE HTIIVEKDSVIVTTE B:  MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKM IMELGGKPAFPVNLSINEIAAHYTPYKGDTTVLKEGDYLK IDVGVHIDGFIADTAVTVRVGMEEDELMEAAKEALNAAIS VARAGVEIKELGKAIENEIRKRGFKPIVNLSGHKIERYKL HAGISIPNIYRPHDNYVLKEGDVFAIEPFATIGAGQVIEV PPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWL QNDMPEGQLKLALKTLEKAGAIYGYPVLKEIRNGIVAQFE HTIIVEKDSVIVTTE Description Functional site 1) chain A residue 82 type sequence D description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A. source : ACA 2) chain A residue 93 type sequence D description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A. source : ACA 3) chain A residue 153 type sequence H description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A. source : ACA 4) chain A residue 187 type sequence E description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A. source : ACA 5) chain A residue 280 type sequence E description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A. source : ACA 6) chain B residue 82 type sequence D description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN B. source : ACB 7) chain B residue 93 type sequence D description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN B. source : ACB 8) chain B residue 153 type sequence H description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN B. source : ACB 9) chain B residue 187 type sequence E description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN B. source : ACB 10) chain B residue 280 type sequence E description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN B. source : ACB 11) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE CO A 296 source : AC1 12) chain A residue 153 type sequence H description BINDING SITE FOR RESIDUE CO A 296 source : AC1 13) chain A residue 187 type sequence E description BINDING SITE FOR RESIDUE CO A 296 source : AC1 14) chain A residue 280 type sequence E description BINDING SITE FOR RESIDUE CO A 296 source : AC1 15) chain A residue 82 type sequence D description BINDING SITE FOR RESIDUE CO A 297 source : AC2 16) chain A residue 93 type sequence D description BINDING SITE FOR RESIDUE CO A 297 source : AC2 17) chain A residue 280 type sequence E description BINDING SITE FOR RESIDUE CO A 297 source : AC2 18) chain B residue 93 type sequence D description BINDING SITE FOR RESIDUE CO B 296 source : AC3 19) chain B residue 153 type sequence H description BINDING SITE FOR RESIDUE CO B 296 source : AC3 20) chain B residue 187 type sequence E description BINDING SITE FOR RESIDUE CO B 296 source : AC3 21) chain B residue 280 type sequence E description BINDING SITE FOR RESIDUE CO B 296 source : AC3 22) chain B residue 82 type sequence D description BINDING SITE FOR RESIDUE CO B 297 source : AC4 23) chain B residue 93 type sequence D description BINDING SITE FOR RESIDUE CO B 297 source : AC4 24) chain B residue 280 type sequence E description BINDING SITE FOR RESIDUE CO B 297 source : AC4 25) chain A residue 82 type catalytic sequence D description 917 source MCSA : MCSA1 26) chain A residue 93 type catalytic sequence D description 917 source MCSA : MCSA1 27) chain A residue 153 type catalytic sequence H description 917 source MCSA : MCSA1 28) chain A residue 161 type catalytic sequence H description 917 source MCSA : MCSA1 29) chain A residue 187 type catalytic sequence E description 917 source MCSA : MCSA1 30) chain A residue 280 type catalytic sequence E description 917 source MCSA : MCSA1 31) chain B residue 82 type catalytic sequence D description 917 source MCSA : MCSA2 32) chain B residue 93 type catalytic sequence D description 917 source MCSA : MCSA2 33) chain B residue 153 type catalytic sequence H description 917 source MCSA : MCSA2 34) chain B residue 161 type catalytic sequence H description 917 source MCSA : MCSA2 35) chain B residue 187 type catalytic sequence E description 917 source MCSA : MCSA2 36) chain B residue 280 type catalytic sequence E description 917 source MCSA : MCSA2 37) chain A residue 62 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01975 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 62 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_01975 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 82 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 40) chain B residue 161 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 41) chain B residue 187 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 42) chain B residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 43) chain A residue 93 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 44) chain A residue 153 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 45) chain A residue 161 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 46) chain A residue 187 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 47) chain A residue 280 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 48) chain B residue 82 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 49) chain B residue 93 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 50) chain B residue 153 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 51) chain A residue 77-93 type prosite sequence DYLKIDVGVHIDGFIAD description MAP_2 Methionine aminopeptidase subfamily 2 signature. DYlKIDvGvHIDGfiaD source prosite : PS01202

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