eF-site ID 1bs6-C PDB Code 1bs6 Chain C click to enlarge Title PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER Classification HYDROLASE Compound PROTEIN (PEPTIDE DEFORMYLASE) Source null (1BS6) Sequence C:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK LDRLKARA Description Functional site 1) 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 2) 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 3) 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 4) chain C residue 1029 type sequence R description BINDING SITE FOR RESIDUE SO4 B 3001 source : AC1 5) chain C residue 1053 type sequence I description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC2 6) chain C residue 1054 type sequence H description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC2 7) chain C residue 1055 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 3002 source : AC2 8) chain C residue 1050 type sequence Q description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 9) chain C residue 1090 type sequence C description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 10) chain C residue 1132 type sequence H description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 11) chain C residue 1136 type sequence H description BINDING SITE FOR RESIDUE NI C 2001 source : AC5 12) chain C residue 1046 type catalytic sequence L description 98 source MCSA : MCSA3 13) chain C residue 1051 type catalytic sequence V description 98 source MCSA : MCSA3 14) chain C residue 1091 type catalytic sequence L description 98 source MCSA : MCSA3 15) chain C residue 1092 type catalytic sequence S description 98 source MCSA : MCSA3 16) chain C residue 1133 type catalytic sequence E description 98 source MCSA : MCSA3 17) chain C residue 1134 type catalytic sequence M description 98 source MCSA : MCSA3 18) chain C residue 1137 type catalytic sequence L description 98 source MCSA : MCSA3 19) chain C residue 1134 type ACT_SITE sequence M description ACT_SITE => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI1 20) chain C residue 1091 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 1133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 1137 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2

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