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4B36

Crystal Structure of Human Angiogenin with an Engineered Loop Exhibits Conformational Flexibility at the Functional Regions of the Molecule

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
B0003676molecular_functionnucleic acid binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1125
ChainResidue
AARG32
AARG33
BARG32
BARG33

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1126
ChainResidue
BHIS13
BASN43
BTHR44
BARG123

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKdiNTF
ChainResidueDetails
ACYS39-PHE45

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMotif: {"description":"Nucleolar localization signal","evidences":[{"source":"PubMed","id":"7945327","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11468363","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38718836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9918722","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11468363","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38718836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9918722","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38718836","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 564
ChainResidueDetails
AHIS13increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
ALYS40electrostatic stabiliser
AHIS116increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 564
ChainResidueDetails
BHIS13increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
BLYS40electrostatic stabiliser
BHIS116increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

246031

PDB entries from 2025-12-10

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