eF-site ID 1g27-ABC PDB Code 1g27 Chain A, B, C click to enlarge Title CRYSTAL STRUCTURE OF E.COLI POLYPEPTIDE DEFORMYLASE COMPLEXED WITH THE INHIBITOR BB-3497 Classification HYDROLASE Compound POLYPEPTIDE DEFORMYLASE Source Escherichia coli (strain K12) (DEF_ECOLI) Sequence A:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK LDRL B:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK LDRL C:  SVLQVLHIPDERLRKVAKPVEEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVIDVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALVPRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGKLFMDYLSPLKQQRIRQKVEK LDRL Description Functional site 1) chain A residue 50 type sequence Q description BINDING SITE FOR RESIDUE NI A 9001 source : AC1 2) chain A residue 90 type sequence C description BINDING SITE FOR RESIDUE NI A 9001 source : AC1 3) chain A residue 132 type sequence H description BINDING SITE FOR RESIDUE NI A 9001 source : AC1 4) chain A residue 136 type sequence H description BINDING SITE FOR RESIDUE NI A 9001 source : AC1 5) chain B residue 50 type sequence Q description BINDING SITE FOR RESIDUE NI B 9002 source : AC2 6) chain B residue 90 type sequence C description BINDING SITE FOR RESIDUE NI B 9002 source : AC2 7) chain B residue 132 type sequence H description BINDING SITE FOR RESIDUE NI B 9002 source : AC2 8) chain B residue 136 type sequence H description BINDING SITE FOR RESIDUE NI B 9002 source : AC2 9) chain C residue 50 type sequence Q description BINDING SITE FOR RESIDUE NI C 9003 source : AC3 10) chain C residue 90 type sequence C description BINDING SITE FOR RESIDUE NI C 9003 source : AC3 11) chain C residue 132 type sequence H description BINDING SITE FOR RESIDUE NI C 9003 source : AC3 12) chain C residue 136 type sequence H description BINDING SITE FOR RESIDUE NI C 9003 source : AC3 13) chain A residue 43 type sequence G description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 14) chain A residue 44 type sequence I description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 15) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 16) chain A residue 50 type sequence Q description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 17) chain A residue 89 type sequence G description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 18) chain A residue 90 type sequence C description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 19) chain A residue 91 type sequence L description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 20) chain A residue 132 type sequence H description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 21) chain A residue 133 type sequence E description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 22) chain A residue 136 type sequence H description BINDING SITE FOR RESIDUE BB1 A 1001 source : AC4 23) chain B residue 43 type sequence G description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 24) chain B residue 44 type sequence I description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 25) chain B residue 45 type sequence G description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 26) chain B residue 50 type sequence Q description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 27) chain B residue 89 type sequence G description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 28) chain B residue 90 type sequence C description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 29) chain B residue 91 type sequence L description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 30) chain B residue 132 type sequence H description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 31) chain B residue 133 type sequence E description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 32) chain B residue 136 type sequence H description BINDING SITE FOR RESIDUE BB1 B 2002 source : AC5 33) chain C residue 43 type sequence G description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 34) chain C residue 44 type sequence I description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 35) chain C residue 45 type sequence G description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 36) chain C residue 50 type sequence Q description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 37) chain C residue 89 type sequence G description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 38) chain C residue 90 type sequence C description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 39) chain C residue 91 type sequence L description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 40) chain C residue 132 type sequence H description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 41) chain C residue 133 type sequence E description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 42) chain C residue 136 type sequence H description BINDING SITE FOR RESIDUE BB1 C 3003 source : AC6 43) chain A residue 46 type catalytic sequence L description 98 source MCSA : MCSA1 44) chain A residue 51 type catalytic sequence V description 98 source MCSA : MCSA1 45) chain A residue 91 type catalytic sequence L description 98 source MCSA : MCSA1 46) chain A residue 92 type catalytic sequence S description 98 source MCSA : MCSA1 47) chain A residue 133 type catalytic sequence E description 98 source MCSA : MCSA1 48) chain A residue 134 type catalytic sequence M description 98 source MCSA : MCSA1 49) chain A residue 137 type catalytic sequence L description 98 source MCSA : MCSA1 50) chain B residue 46 type catalytic sequence L description 98 source MCSA : MCSA2 51) chain B residue 51 type catalytic sequence V description 98 source MCSA : MCSA2 52) chain B residue 91 type catalytic sequence L description 98 source MCSA : MCSA2 53) chain B residue 92 type catalytic sequence S description 98 source MCSA : MCSA2 54) chain B residue 133 type catalytic sequence E description 98 source MCSA : MCSA2 55) chain B residue 134 type catalytic sequence M description 98 source MCSA : MCSA2 56) chain B residue 137 type catalytic sequence L description 98 source MCSA : MCSA2 57) chain C residue 46 type catalytic sequence L description 98 source MCSA : MCSA3 58) chain C residue 51 type catalytic sequence V description 98 source MCSA : MCSA3 59) chain C residue 91 type catalytic sequence L description 98 source MCSA : MCSA3 60) chain C residue 92 type catalytic sequence S description 98 source MCSA : MCSA3 61) chain C residue 133 type catalytic sequence E description 98 source MCSA : MCSA3 62) chain C residue 134 type catalytic sequence M description 98 source MCSA : MCSA3 63) chain C residue 137 type catalytic sequence L description 98 source MCSA : MCSA3 64) chain A residue 134 type ACT_SITE sequence M description ACT_SITE => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 134 type ACT_SITE sequence M description ACT_SITE => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI1 66) chain C residue 134 type ACT_SITE sequence M description ACT_SITE => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 91 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 68) chain A residue 133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 137 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 70) chain B residue 91 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 71) chain B residue 133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 72) chain B residue 137 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 73) chain C residue 91 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 74) chain C residue 133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2 75) chain C residue 137 type BINDING sequence L description BINDING => ECO:0000269|PubMed:9846875 source Swiss-Prot : SWS_FT_FI2

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