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1X1C

Crystal structure of BchU complexed with S-adenosyl-L-homocysteine and Zn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008168molecular_functionmethyltransferase activity
A0008171molecular_functionO-methyltransferase activity
A0015995biological_processchlorophyll biosynthetic process
A0016740molecular_functiontransferase activity
A0030494biological_processbacteriochlorophyll biosynthetic process
A0032259biological_processmethylation
A0036069biological_processlight-dependent bacteriochlorophyll biosynthetic process
A0036070biological_processlight-independent bacteriochlorophyll biosynthetic process
A0046872molecular_functionmetal ion binding
A0046983molecular_functionprotein dimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 5001
ChainResidue
AHIS150
AHIS290

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 5002
ChainResidue
AASP286
AHIS290

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN A 5003
ChainResidue
AHIS190

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 5005
ChainResidue
AHIS11
AASP329

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 4396
ChainResidue
AGLU84
AASN74
ATHR83

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SAH A 4261
ChainResidue
ATYR135
AGLU147
AHIS150
AGLY177
AGLY179
AILE183
AASN200
ALEU201
AVAL226
AASP227
AILE228
ATYR229
ACYS242
AARG243
AILE244
AHOH5020

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 2431
ChainResidue
AARG140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1X1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X1B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X1C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1X1D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16797589","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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

239492

PDB entries from 2025-07-30

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