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6C07

Crystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004478molecular_functionmethionine adenosyltransferase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006556biological_processS-adenosylmethionine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0004478molecular_functionmethionine adenosyltransferase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006556biological_processS-adenosylmethionine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0004478molecular_functionmethionine adenosyltransferase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006556biological_processS-adenosylmethionine biosynthetic process
C0006730biological_processone-carbon metabolic process
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0004478molecular_functionmethionine adenosyltransferase activity
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006556biological_processS-adenosylmethionine biosynthetic process
D0006730biological_processone-carbon metabolic process
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CL A 501
ChainResidue
AGLY288
AALA289
ALYS293
BARG272
BHOH714

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
AHOH786
BHOH643
AASP266
AALA267
AHOH682
AHOH692

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 503
ChainResidue
AASP139
AHOH632
AHOH729
AHOH773
AHOH822
BHOH679

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 501
ChainResidue
BGLY182
BHOH647
BHOH694
BHOH766
BHOH795
BHOH811

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 502
ChainResidue
AHOH698
BASP266
BALA267
BHOH671
BHOH705
BHOH763

site_idAC6
Number of Residues4
Detailsbinding site for residue K C 501
ChainResidue
CGLY271
DGLY271
DHOH709
DHOH776

site_idAC7
Number of Residues5
Detailsbinding site for residue CL C 502
ChainResidue
CHIS34
CLYS189
CLYS273
CHOH797
CHOH824

site_idAC8
Number of Residues6
Detailsbinding site for residue MG C 503
ChainResidue
CASP266
CALA267
CHOH609
CHOH653
CHOH845
DHOH642

site_idAC9
Number of Residues6
Detailsbinding site for residue MG C 504
ChainResidue
CASP139
CHOH642
CHOH703
CHOH747
CHOH832
DHOH638

site_idAD1
Number of Residues7
Detailsbinding site for residue MG D 501
ChainResidue
DASP36
DLYS273
DHOH615
DHOH639
DHOH653
DHOH686
DHOH803

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGrFTIGGP
ChainResidueDetails
APRO254-PRO263

site_idPS00376
Number of Residues11
DetailsADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGmmfGY
ChainResidueDetails
AGLY136-TYR146

site_idPS00377
Number of Residues9
DetailsADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD
ChainResidueDetails
AGLY286-ASP294

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PDB entries from 2024-09-04

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