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1X1A

Crystal structure of BchU complexed with S-adenosyl-L-methionine

Functional Information from GO Data
ChainGOidnamespacecontents
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0030494biological_processbacteriochlorophyll biosynthetic process
A0032259biological_processmethylation
A0036069biological_processlight-dependent bacteriochlorophyll biosynthetic process
A0036070biological_processlight-independent bacteriochlorophyll biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 4396
ChainResidue
AASN74
AGLU84

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SAM A 4264
ChainResidue
AASP227
AILE228
ATYR229
ACYS242
AARG243
AHOH4452
AHOH4460
AGLU147
AHIS150
AGLY177
AGLY179
AASN200
ALEU201
AVAL226

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 2431
ChainResidue
AARG140
AHOH4461

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:16797589
ChainResidueDetails
ATYR246

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:16797589, ECO:0007744|PDB:1X1A, ECO:0007744|PDB:1X1B, ECO:0007744|PDB:1X1C, ECO:0007744|PDB:1X1D
ChainResidueDetails
AGLU147
AGLY177
AASN200
AASP227
ACYS242

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:16797589
ChainResidueDetails
AHIS150

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000305|PubMed:16797589
ChainResidueDetails
AHIS290

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kyw
ChainResidueDetails
ATYR246

222415

PDB entries from 2024-07-10

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