Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1H0D

Crystal structure of Human Angiogenin in complex with Fab fragment of its monoclonal antibody mAb 26-2F

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0001525	biological_process	angiogenesis
C	0001541	biological_process	ovarian follicle development
C	0001556	biological_process	oocyte maturation
C	0001666	biological_process	response to hypoxia
C	0001890	biological_process	placenta development
C	0001938	biological_process	positive regulation of endothelial cell proliferation
C	0003676	molecular_function	nucleic acid binding
C	0003677	molecular_function	DNA binding
C	0003779	molecular_function	actin binding
C	0004518	molecular_function	nuclease activity
C	0004519	molecular_function	endonuclease activity
C	0004521	molecular_function	RNA endonuclease activity
C	0004540	molecular_function	RNA nuclease activity
C	0004549	molecular_function	tRNA-specific ribonuclease activity
C	0005102	molecular_function	signaling receptor binding
C	0005507	molecular_function	copper ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005604	cellular_component	basement membrane
C	0005615	cellular_component	extracellular space
C	0005634	cellular_component	nucleus
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0007154	biological_process	cell communication
C	0007165	biological_process	signal transduction
C	0008201	molecular_function	heparin binding
C	0009303	biological_process	rRNA transcription
C	0009725	biological_process	response to hormone
C	0010494	cellular_component	cytoplasmic stress granule
C	0016078	biological_process	tRNA decay
C	0016477	biological_process	cell migration
C	0016787	molecular_function	hydrolase activity
C	0017148	biological_process	negative regulation of translation
C	0019731	biological_process	antibacterial humoral response
C	0019843	molecular_function	rRNA binding
C	0023052	biological_process	signaling
C	0030041	biological_process	actin filament polymerization
C	0030139	cellular_component	endocytic vesicle
C	0030154	biological_process	cell differentiation
C	0030426	cellular_component	growth cone
C	0032055	biological_process	negative regulation of translation in response to stress
C	0032311	cellular_component	angiogenin-PRI complex
C	0034063	biological_process	stress granule assembly
C	0042277	molecular_function	peptide binding
C	0042327	biological_process	positive regulation of phosphorylation
C	0042592	biological_process	homeostatic process
C	0042803	molecular_function	protein homodimerization activity
C	0043022	molecular_function	ribosome binding
C	0043025	cellular_component	neuronal cell body
C	0043066	biological_process	negative regulation of apoptotic process
C	0045087	biological_process	innate immune response
C	0048018	molecular_function	receptor ligand activity
C	0048662	biological_process	negative regulation of smooth muscle cell proliferation
C	0050714	biological_process	positive regulation of protein secretion
C	0050830	biological_process	defense response to Gram-positive bacterium
C	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
C	0071425	biological_process	hematopoietic stem cell proliferation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1212

Chain	Residue
A	SER14
A	LYS106
A	HOH2130
C	SER4
C	ARG5

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 1216

Chain	Residue
B	HOH2034
B	HOH2104
C	ARG21
B	GLY53
B	GLY54
B	ARG71
B	ILE73

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 1124

Chain	Residue
A	HOH2101
C	HIS13
C	LYS40
C	HOH2092
C	HOH2093

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 1125

Chain	Residue
C	ASN49
C	LYS50
C	ARG51
C	HOH2011

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 1126

Chain	Residue
C	HIS65
C	ARG66

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 1127

Chain	Residue
C	TYR6
C	LYS50
C	LYS54

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 1128

Chain	Residue
C	ARG32
C	ARG33

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 1129

Chain	Residue
C	LYS60
C	ASN63
C	HIS65

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 1213

Chain	Residue
A	SER55
A	ARG208

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 1214

Chain	Residue
A	SER64
A	GLY65
A	SER66
A	HOH2055

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1215

Chain	Residue
A	PRO8
A	ALA9
A	SER10

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1216

Chain	Residue
A	THR163
A	ASP164
A	ASP166
A	HOH2110
A	HOH2112
B	HIS164

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B 1217

Chain	Residue
A	GLU122
B	SER120
B	VAL121
B	TYR122
B	SER202
B	SER203
B	LYS208
B	HOH2098

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 1218

Chain	Residue
A	GLN123
A	SER126
B	TYR122
B	LYS143

Functional Information from PROSITE/UniProt

site_id	PS00127
Number of Residues	7
Details	RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKdiNTF

Chain	Residue	Details
C	CYS39-PHE45

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH

Chain	Residue	Details
A	TYR191-HIS197

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Motif: {"description":"Nucleolar localization signal","evidences":[{"source":"PubMed","id":"7945327","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"38718836","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1a4y

Chain	Residue	Details
C	HIS13
C	LYS40
C	HIS114

site_id	MCSA1
Number of Residues	3
Details	M-CSA 564

Chain	Residue	Details
C	LYS17	increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
C	THR44	electrostatic stabiliser
C	SER118	increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)