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1K5B

Crystal Structure of Human Angiogenin Variant des(121-123)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001541biological_processovarian follicle development
A0001556biological_processoocyte maturation
A0001666biological_processresponse to hypoxia
A0001890biological_processplacenta development
A0001938biological_processpositive regulation of endothelial cell proliferation
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003779molecular_functionactin binding
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0004549molecular_functiontRNA-specific ribonuclease activity
A0005102molecular_functionsignaling receptor binding
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007154biological_processcell communication
A0007165biological_processsignal transduction
A0008201molecular_functionheparin binding
A0009303biological_processrRNA transcription
A0009725biological_processresponse to hormone
A0010494cellular_componentcytoplasmic stress granule
A0015629cellular_componentactin cytoskeleton
A0016078biological_processtRNA decay
A0016477biological_processcell migration
A0017148biological_processnegative regulation of translation
A0019731biological_processantibacterial humoral response
A0019843molecular_functionrRNA binding
A0023052biological_processsignaling
A0030041biological_processactin filament polymerization
A0030139cellular_componentendocytic vesicle
A0030154biological_processcell differentiation
A0030426cellular_componentgrowth cone
A0032055biological_processnegative regulation of translation in response to stress
A0032311cellular_componentangiogenin-PRI complex
A0034063biological_processstress granule assembly
A0042277molecular_functionpeptide binding
A0042327biological_processpositive regulation of phosphorylation
A0042592biological_processhomeostatic process
A0042803molecular_functionprotein homodimerization activity
A0043022molecular_functionribosome binding
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0045087biological_processinnate immune response
A0048018molecular_functionreceptor ligand activity
A0048662biological_processnegative regulation of smooth muscle cell proliferation
A0050714biological_processpositive regulation of protein secretion
A0050830biological_processdefense response to Gram-positive bacterium
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A0071425biological_processhematopoietic stem cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CIT A 121
ChainResidue
AASP41
AASN49
AARG51
ASER52
ALYS82
ALEU83
AARG95

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11468363, ECO:0000269|PubMed:38718836, ECO:0000269|PubMed:9918722
ChainResidueDetails
AHIS13

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11468363, ECO:0000269|PubMed:38718836, ECO:0000269|PubMed:9918722
ChainResidueDetails
AHIS114

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:38718836
ChainResidueDetails
AARG21
AASP22
ACYS81
AVAL103

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:2866794
ChainResidueDetails
APCA1

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4y
ChainResidueDetails
AHIS13
ALYS40
AHIS114

site_idMCSA1
Number of Residues3
DetailsM-CSA 564
ChainResidueDetails
AHIS13increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
ALYS40electrostatic stabiliser
AHIS114increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

229380

PDB entries from 2024-12-25

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