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5DMM

Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Metallated form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006974biological_processDNA damage response
A0008168molecular_functionmethyltransferase activity
A0008270molecular_functionzinc ion binding
A0008898molecular_functionS-adenosylmethionine-homocysteine S-methyltransferase activity
A0009086biological_processmethionine biosynthetic process
A0032259biological_processmethylation
A0033477biological_processS-methylmethionine metabolic process
A0033528biological_processS-methylmethionine cycle
A0046872molecular_functionmetal ion binding
A0061627molecular_functionS-methylmethionine-homocysteine S-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 501
ChainResidue
ACYS229
AASN255
ACYS295
ACYS296
AHCS505

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
AGLU104
AASP138
AHIS140
AHOH745

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 503
ChainResidue
AGLU109
AGLU144
AHOH738
AHOH741

site_idAC4
Number of Residues3
Detailsbinding site for residue BME A 504
ChainResidue
AALA24
ACYS296
AARG297

site_idAC5
Number of Residues8
Detailsbinding site for residue HCS A 505
ChainResidue
AILE67
ATYR71
ASER121
AGLU168
ATHR169
ACYS229
AZN501
AHOH606

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00333
ChainResidueDetails
ACYS229
ACYS295
ACYS296

219515

PDB entries from 2024-05-08

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