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2NQ5

Crystal structure of methyltransferase from Streptococcus mutans

Functional Information from GO Data
ChainGOidnamespacecontents
A0003871molecular_function5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
A0008168molecular_functionmethyltransferase activity
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0009086biological_processmethionine biosynthetic process
A0032259biological_processmethylation
A0046872molecular_functionmetal ion binding
A0071266biological_process'de novo' L-methionine biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P82610
ChainResidueDetails
AHIS683

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P82610
ChainResidueDetails
ALYS19
AASN115
AILE420
AGLU473
AASP478
ATYR501
AARG504
ATRP550
AASP588

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00172, ECO:0000269|PubMed:21840320, ECO:0007744|PDB:3T0C
ChainResidueDetails
AHIS630
ACYS632
ACYS715

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21840320, ECO:0007744|PDB:3T0C
ChainResidueDetails
AGLU654

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uro
ChainResidueDetails
AGLU475
ATRP550

227344

PDB entries from 2024-11-13

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