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1K7Y

E. coli MetH C-terminal fragment (649-1227)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008705molecular_functionmethionine synthase activity
A0009086biological_processmethionine biosynthetic process
A0031419molecular_functioncobalamin binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 254
ChainResidue
ALYS712
AHIS927
AARG928

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 255
ChainResidue
ASO4282
ALYS755
APRO785
AALA786
AGLU787
AASN816

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 267
ChainResidue
AARG928
AGLN932
AARG1106
ATYR1111

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 323
ChainResidue
ATYR1139
AB121248

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 251
ChainResidue
ALYS720
AARG723
ATYR1083

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 259
ChainResidue
ALYS819
ALYS1188

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 260
ChainResidue
AARG823
APRO1140
AB121248

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 270
ChainResidue
AARG996
AHIS1160

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 282
ChainResidue
ASO4255
AARG1127

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 309
ChainResidue
AVAL971

site_idBC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE B12 A 1248
ChainResidue
ASO4260
AHOH271
AHOH279
ASO4323
AVAL758
AGLY762
AILE765
AVAL766
AGLY802
ALEU803
ASER804
ALEU806
AILE807
ATHR808
ALEU831
AGLY833
AGLY834
AALA835
ATHR836
AVAL857
AGLN858
AASN859
AALA860
ATHR863
AASP1093
AALA1136
APRO1137
AGLY1138
ATYR1139
APRO1140
AHIS1145
AALA1170
AMET1171
AGLY1174
AALA1175
ASER1176
AVAL1177
ASER1178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:7992050, ECO:0007744|PDB:1BMT
ChainResidueDetails
AGLU694
AGLY756
ASER804
ATHR808
AALA860

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:7992050, ECO:0007744|PDB:1BMT
ChainResidueDetails
AGLY759

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:8939751
ChainResidueDetails
AASP946
AARG1134
ATYR1189

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 268
ChainResidueDetails
AASP757hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AGLY759hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, increase nucleophilicity, metal ligand, proton acceptor, proton donor
ASER810hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
ASER810
AASP757
AGLY759

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bmt
ChainResidueDetails
ALEU770

219140

PDB entries from 2024-05-01

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