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2FCC

Crystal Structure of T4 Pyrimidine Dimer Glycosylase (T4-Pdg) Covalently Complexed with a DNA Substrate Containing Abasic Site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000704molecular_functionpyrimidine dimer DNA N-glycosylase activity
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0004519molecular_functionendonuclease activity
A0006281biological_processDNA repair
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016829molecular_functionlyase activity
A0033959molecular_functiondeoxyribodipyrimidine endonucleosidase activity
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
B0000704molecular_functionpyrimidine dimer DNA N-glycosylase activity
B0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
B0004519molecular_functionendonuclease activity
B0006281biological_processDNA repair
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016829molecular_functionlyase activity
B0033959molecular_functiondeoxyribodipyrimidine endonucleosidase activity
B0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ATHR49
APHE50
ATYR104
APRO106
AHIS107
ASER110
AHOH1080

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AGLN124
AARG117
ALYS121

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 601
ChainResidue
BTHR49
BPHE50
BPHE59
BTYR104
BPRO106
BHIS107
BSER110

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
APHE66
ALYS69
AARG70
AGLU73
AHOH1044
AHOH1088

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile; via amide nitrogen => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS
ChainResidueDetails
AGLU23
BGLU23

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Substrate binding => ECO:0000269|PubMed:1409651, ECO:0000269|PubMed:7783199
ChainResidueDetails
AARG3
BARG3

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Substrate binding => ECO:0000269|PubMed:1409651
ChainResidueDetails
AARG22
AARG117
ALYS121
BARG22
BARG117
BLYS121

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0007744|PDB:1VAS
ChainResidueDetails
AARG26
BARG26

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1vas
ChainResidueDetails
AARG22
ATHR2
AGLU23
AARG26

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1vas
ChainResidueDetails
BARG22
BTHR2
BGLU23
BARG26

site_idMCSA1
Number of Residues4
DetailsM-CSA 162
ChainResidueDetails
ATHR2covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AARG22electrostatic stabiliser, hydrogen bond donor
AGLU23hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG26electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 162
ChainResidueDetails
BTHR2covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BARG22electrostatic stabiliser, hydrogen bond donor
BGLU23hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG26electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-06-26

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