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1B49

DCMP HYDROXYMETHYLASE FROM T4 (PHOSPHATE-BOUND)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016740molecular_functiontransferase activity
A0047153molecular_functiondeoxycytidylate 5-hydroxymethyltransferase activity
A0052031biological_processsymbiont-mediated perturbation of host defense response
A0052170biological_processsymbiont-mediated suppression of host innate immune response
A0099018biological_processsymbiont-mediated evasion of host restriction-modification system
C0016740molecular_functiontransferase activity
C0047153molecular_functiondeoxycytidylate 5-hydroxymethyltransferase activity
C0052031biological_processsymbiont-mediated perturbation of host defense response
C0052170biological_processsymbiont-mediated suppression of host innate immune response
C0099018biological_processsymbiont-mediated evasion of host restriction-modification system
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 300
ChainResidue
ALYS28
AARG168
ASER169
AHOH314
CARG123
CARG124
CHOH302

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 C 301
ChainResidue
AARG123
AARG124
AHOH321
CLYS28
CARG168
CSER169
CHOH316

site_idCAT
Number of Residues2
Details
ChainResidue
ACYS148
CCYS148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10064578","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10064578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1420151","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10064578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1420151","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1B5D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1B5E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6A9A","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10064578","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6A9A","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10064578","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1B5E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6A9A","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10064578","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B5D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1B5E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
AASP179
AGLN183
ACYS148

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b02
ChainResidueDetails
CASP179
CGLN183
CCYS148

site_idMCSA1
Number of Residues3
DetailsM-CSA 700
ChainResidueDetails
AGLU60electrostatic stabiliser, proton acceptor, proton donor
ACYS148covalently attached, nucleofuge, nucleophile
AASP179electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 700
ChainResidueDetails

248942

PDB entries from 2026-02-11

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