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4HUP

Structure of ricin A chain bound with N-(N-(pterin-7-yl)carbonylglycyl)-L-phenylalanyl)-L-phenylalanine

Functional Information from GO Data
ChainGOidnamespacecontents
X0017148biological_processnegative regulation of translation
X0030598molecular_functionrRNA N-glycosylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 19M X 301
ChainResidue
XALA79
XARG180
XASN209
XGLY212
XHOH401
XHOH403
XHOH405
XHOH696
XTYR80
XVAL81
XPHE93
XGLY121
XASN122
XTYR123
XILE172
XSER176

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 X 302
ChainResidue
XTHR17
XGLN19
XHIS65
XHOH445
XHOH607
XHOH625

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 X 303
ChainResidue
XPHE119
XGLY120
XARG125
XHOH408
XHOH524
XHOH668
XHOH721

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLA X 304
ChainResidue
XASN195
XARG196
XARG197
XHOH484
XHOH595
XHOH610
XHOH729

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLA X 305
ChainResidue
XTYR194
XGLY212
XARG213
XTHR216
XARG258
XHOH521
XHOH535
XHOH723

Functional Information from PROSITE/UniProt
site_idPS00275
Number of Residues17
DetailsSHIGA_RICIN Shiga/ricin ribosomal inactivating toxins active site signature. IqMIsEAARFQyIEgeM
ChainResidueDetails
XILE172-MET188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P84531","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8780513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OBT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000080","evidences":[{"source":"PubMed","id":"1368517","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","featureId":"CAR_000081","evidences":[{"source":"PubMed","id":"1368517","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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