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1T7L

Crystal Structure of Cobalamin-Independent Methionine Synthase from T. maritima

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_processobsolete methionine biosynthetic process
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0046872molecular_functionmetal ion binding
A0071266biological_process'de novo' L-methionine biosynthetic process
B0003871molecular_function5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
B0008168molecular_functionmethyltransferase activity
B0008270molecular_functionzinc ion binding
B0008652biological_processamino acid biosynthetic process
B0009086biological_processobsolete methionine biosynthetic process
B0016740molecular_functiontransferase activity
B0032259biological_processmethylation
B0046872molecular_functionmetal ion binding
B0071266biological_process'de novo' L-methionine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1350
ChainResidue
AARG85
ATYR388
AARG391
AGLU635
ALYS662
AHOH1145

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1351
ChainResidue
BARG391
BGLU635
BLYS662
BHOH1466
BARG85
BGLU387
BTYR388

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MRY B 1352
ChainResidue
BLYS104
BPHE106
BLEU156
BCYS205
BILE587
BHOH1392
BHOH1510
BHOH1590

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MRY A 1353
ChainResidue
ALYS104
APHE106
ALEU156
ACYS205
AILE587
AHOH854
AHOH905
AHOH1257
AHOH1322

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P82610","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XR2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P82610","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XR2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18296644","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BQ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BQ6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18296644","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BQ6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uro
ChainResidueDetails
ATRP539
AGLU464

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1uro
ChainResidueDetails
BTRP539
BGLU464

249524

PDB entries from 2026-02-18

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