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3TSR

X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0009617biological_processresponse to bacterium
A0016829molecular_functionlyase activity
A0050830biological_processdefense response to Gram-positive bacterium
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0004522molecular_functionribonuclease A activity
B0004540molecular_functionRNA nuclease activity
B0005576cellular_componentextracellular region
B0009617biological_processresponse to bacterium
B0016829molecular_functionlyase activity
B0050830biological_processdefense response to Gram-positive bacterium
C0003676molecular_functionnucleic acid binding
C0004519molecular_functionendonuclease activity
C0004522molecular_functionribonuclease A activity
C0004540molecular_functionRNA nuclease activity
C0005576cellular_componentextracellular region
C0009617biological_processresponse to bacterium
C0016829molecular_functionlyase activity
C0050830biological_processdefense response to Gram-positive bacterium
D0003676molecular_functionnucleic acid binding
D0004519molecular_functionendonuclease activity
D0004522molecular_functionribonuclease A activity
D0004540molecular_functionRNA nuclease activity
D0005576cellular_componentextracellular region
D0009617biological_processresponse to bacterium
D0016829molecular_functionlyase activity
D0050830biological_processdefense response to Gram-positive bacterium
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005886cellular_componentplasma membrane
E0008428molecular_functionribonuclease inhibitor activity
E0016477biological_processcell migration
E0030027cellular_componentlamellipodium
E0032311cellular_componentangiogenin-PRI complex
E0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
E0045765biological_processregulation of angiogenesis
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005886cellular_componentplasma membrane
F0008428molecular_functionribonuclease inhibitor activity
F0016477biological_processcell migration
F0030027cellular_componentlamellipodium
F0032311cellular_componentangiogenin-PRI complex
F0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
F0045765biological_processregulation of angiogenesis
G0005654cellular_componentnucleoplasm
G0005737cellular_componentcytoplasm
G0005886cellular_componentplasma membrane
G0008428molecular_functionribonuclease inhibitor activity
G0016477biological_processcell migration
G0030027cellular_componentlamellipodium
G0032311cellular_componentangiogenin-PRI complex
G0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
G0045765biological_processregulation of angiogenesis
H0005654cellular_componentnucleoplasm
H0005737cellular_componentcytoplasm
H0005886cellular_componentplasma membrane
H0008428molecular_functionribonuclease inhibitor activity
H0016477biological_processcell migration
H0030027cellular_componentlamellipodium
H0032311cellular_componentangiogenin-PRI complex
H0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
H0045765biological_processregulation of angiogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 126
ChainResidue
AGLN29
AHOH631
EASN89

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG E 457
ChainResidue
ELYS269
EASP270
EARG273
HGLU94
HALA95
HLEU127

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO E 458
ChainResidue
ESER231
EASN232
ELYS233
EGLU260
EASP262

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO E 459
ChainResidue
EGLU8
EGLN9
EASP32

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO F 457
ChainResidue
FSER231
FASN232
FLYS233
FGLU260
FASP262

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO F 458
ChainResidue
BGLN29
FASN89
FHOH926

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO F 459
ChainResidue
BARG33
FGLN9

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO G 457
ChainResidue
GSER231
GASN232
GLYS233
GGLU260

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO G 458
ChainResidue
GGLU62
GASN89

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO G 459
ChainResidue
GSER383
GHOH870

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO G 460
ChainResidue
GCYS7
GGLN9
GASP32

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO H 457
ChainResidue
HASN61
HGLU62
HASN89

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO H 458
ChainResidue
HSER383

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO H 459
ChainResidue
DARG33
HGLN9

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF
ChainResidueDetails
ACYS41-PHE47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P10775
ChainResidueDetails
EMET1
FMET1
GMET1
HMET1

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13489
ChainResidueDetails
ESER86
FSER86
GSER86
HSER86

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
DLYS8
DARG11
DLYS42
DLYS67
ALYS8
AARG11
ALYS42
ALYS67
BLYS8
BARG11
BLYS42
BLYS67
CLYS8
CARG11
CLYS42
CLYS67

221051

PDB entries from 2024-06-12

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