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3LE7

Crystal structure of PD-L1 from P. dioica in complex with adenine

Functional Information from GO Data
ChainGOidnamespacecontents
A0006952biological_processdefense response
A0016787molecular_functionhydrolase activity
A0017148biological_processnegative regulation of translation
A0030598molecular_functionrRNA N-glycosylase activity
A0035821biological_processmodulation of process of another organism
A0090729molecular_functiontoxin activity
B0006952biological_processdefense response
B0016787molecular_functionhydrolase activity
B0017148biological_processnegative regulation of translation
B0030598molecular_functionrRNA N-glycosylase activity
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS00275
Number of Residues17
DetailsSHIGA_RICIN Shiga/ricin ribosomal inactivating toxins active site signature. IqMVsEAARFKyIEnqV
ChainResidueDetails
AILE173-VAL189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P84531
ChainResidueDetails
ATYR75
ATYR125
AGLU178
AARG181
BTYR75
BTYR125
BGLU178
BARG181

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20174685, ECO:0007744|PDB:3LE7
ChainResidueDetails
AVAL76
ASER123
AARG181
BVAL76
BSER123
BARG181

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in PD-L1 and PD-L2 => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:19014994, ECO:0000269|PubMed:19452522, ECO:0000269|PubMed:20174685, ECO:0007744|PDB:3H5K, ECO:0007744|PDB:3LE7
ChainResidueDetails
AASN13
BASN13

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in PD-L1 and PD-L2 => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:10213004, ECO:0000269|PubMed:19014994
ChainResidueDetails
AASN46
BASN46

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in PD-L1 => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:19014994
ChainResidueDetails
AASN258
BASN258

226707

PDB entries from 2024-10-30

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