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1U1H

A. thaliana cobalamine independent methionine synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000325cellular_componentplant-type vacuole
A0003729molecular_functionmRNA binding
A0003871molecular_function5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006346biological_processDNA methylation-dependent heterochromatin formation
A0008168molecular_functionmethyltransferase activity
A0008172molecular_functionS-methyltransferase activity
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0008705molecular_functionmethionine synthase activity
A0009086biological_processmethionine biosynthetic process
A0009506cellular_componentplasmodesma
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0010043biological_processresponse to zinc ion
A0032259biological_processmethylation
A0046872molecular_functionmetal ion binding
A0048046cellular_componentapoplast
A0051574biological_processobsolete positive regulation of histone H3-K9 methylation
A0071266biological_process'de novo' L-methionine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 766
ChainResidue
AHIS647
ACYS649
ACYS733
AMET772
AHOH773

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 767
ChainResidue
AHIS135
AGLU194
AHIS658
AASP662

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 768
ChainResidue
APRO79
APRO80
AARG81
AHOH798

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 769
ChainResidue
AARG610
ATYR650
ASER651
AHIS652

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 770
ChainResidue
ALYS55
APHE56
AASP150
ATHR201

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 771
ChainResidue
APRO575
AARG576
AHIS577
ATRP626

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MET A 772
ChainResidue
AILE437
AGLY438
ASER439
AGLU490
AMSE496
AMSE557
AASP605
AHIS647
ACYS649
AGLY734
AZN766

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P82610
ChainResidueDetails
AHIS701

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15326182, ECO:0007744|PDB:1U1J, ECO:0007744|PDB:1U22
ChainResidueDetails
ALYS18
AARG521
ATRP567

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15326182, ECO:0007744|PDB:1U1J
ChainResidueDetails
AASN116

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15326182, ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J
ChainResidueDetails
AILE437
AGLU490
AASP605

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15326182, ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, ECO:0007744|PDB:1U1U, ECO:0007744|PDB:1U22
ChainResidueDetails
AHIS647
AHIS658
AASP662

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15326182, ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, ECO:0007744|PDB:1U22
ChainResidueDetails
ACYS649
ACYS733

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P82610
ChainResidueDetails
AGLU671

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PDB entries from 2024-07-24

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