eF-site ID 1bs6-ABCDEF PDB Code 1bs6 Chain A, B, C, D, E, F click to enlarge Title PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER Classification HYDROLASE Compound PROTEIN (PEPTIDE DEFORMYLASE) Source Escherichia coli (strain K12) (1BS6) Sequence A:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK LDRLKARA B:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK LDRLKARA C:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK LDRLKARA D:  MAS E:  MAS F:  MAS Description Functional site 1) chain A residue 90 type sequence C description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN A source : NIA 2) chain A residue 132 type sequence H description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN A source : NIA 3) chain A residue 136 type sequence H description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN A source : NIA 4) chain B residue 590 type sequence C description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN B source : NIB 5) chain B residue 632 type sequence H description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN B source : NIB 6) chain B residue 636 type sequence H description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN B source : NIB 7) chain C residue 1090 type sequence C description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN C source : NIC 8) chain C residue 1132 type sequence H description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN C source : NIC 9) chain C residue 1136 type sequence H description ONE TRIPEPTIDE MET-ALA-SER IS LOCATED IN ACTIVE SITE NEAR NICKEL ION FOR CHAIN C source : NIC 10) chain B residue 554 type sequence H description BINDING SITE FOR RESIDUE SO4 B 3001 source : AC1 11) chain B residue 555 type sequence Q description BINDING SITE FOR RESIDUE SO4 B 3001 source : AC1 12) chain C residue 1029 type sequence R description BINDING SITE FOR RESIDUE SO4 B 3001 source : AC1 13) chain B residue 529 type sequence R description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC2 14) chain C residue 1053 type sequence I description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC2 15) chain C residue 1054 type sequence H description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC2 16) chain C residue 1055 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC2 17) chain A residue 90 type sequence C description BINDING SITE FOR RESIDUE NI A 2001 source : AC3 18) chain A residue 132 type sequence H description BINDING SITE FOR RESIDUE NI A 2001 source : AC3 19) chain A residue 136 type sequence H description BINDING SITE FOR RESIDUE NI A 2001 source : AC3 20) chain B residue 550 type sequence Q description BINDING SITE FOR RESIDUE NI B 2001 source : AC4 21) chain B residue 590 type sequence C description BINDING SITE FOR RESIDUE NI B 2001 source : AC4 22) chain B residue 632 type sequence H description BINDING SITE FOR RESIDUE NI B 2001 source : AC4 23) chain B residue 636 type sequence H description BINDING SITE FOR RESIDUE NI B 2001 source : AC4 24) chain E residue 1 type sequence M description BINDING SITE FOR RESIDUE NI B 2001 source : AC4 25) chain C residue 1050 type sequence Q description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 26) chain C residue 1090 type sequence C description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 27) chain C residue 1132 type sequence H description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 28) chain C residue 1136 type sequence H description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 29) chain A residue 46 type catalytic sequence L description 98 source MCSA : MCSA1 30) chain A residue 51 type catalytic sequence V description 98 source MCSA : MCSA1 31) chain A residue 91 type catalytic sequence L description 98 source MCSA : MCSA1 32) chain A residue 92 type catalytic sequence S description 98 source MCSA : MCSA1 33) chain A residue 133 type catalytic sequence E description 98 source MCSA : MCSA1 34) chain A residue 134 type catalytic sequence M description 98 source MCSA : MCSA1 35) chain A residue 137 type catalytic sequence L description 98 source MCSA : MCSA1 36) chain B residue 546 type catalytic sequence L description 98 source MCSA : MCSA2 37) chain B residue 551 type catalytic sequence V description 98 source MCSA : MCSA2 38) chain B residue 591 type catalytic sequence L description 98 source MCSA : MCSA2 39) chain B residue 592 type catalytic sequence S description 98 source MCSA : MCSA2 40) chain B residue 633 type catalytic sequence E description 98 source MCSA : MCSA2 41) chain B residue 634 type catalytic sequence M description 98 source MCSA : MCSA2 42) chain B residue 637 type catalytic sequence L description 98 source MCSA : MCSA2 43) chain C residue 1046 type catalytic sequence L description 98 source MCSA : MCSA3 44) chain C residue 1051 type catalytic sequence V description 98 source MCSA : MCSA3 45) chain C residue 1091 type catalytic sequence L description 98 source MCSA : MCSA3 46) chain C residue 1092 type catalytic sequence S description 98 source MCSA : MCSA3 47) chain C residue 1133 type catalytic sequence E description 98 source MCSA : MCSA3 48) chain C residue 1134 type catalytic sequence M description 98 source MCSA : MCSA3 49) chain C residue 1137 type catalytic sequence L description 98 source MCSA : MCSA3 50) chain A residue 134 type ACT_SITE sequence M description ACT_SITE => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 634 type ACT_SITE sequence M description ACT_SITE => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI1 52) chain C residue 1134 type ACT_SITE sequence M description ACT_SITE => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 91 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 137 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 591 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 633 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 637 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 59) chain C residue 1091 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 60) chain C residue 1133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 61) chain C residue 1137 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2

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