3TSR
X-ray structure of mouse ribonuclease inhibitor complexed with mouse ribonuclease 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004522 | molecular_function | ribonuclease A activity |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0009617 | biological_process | response to bacterium |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004522 | molecular_function | ribonuclease A activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0009617 | biological_process | response to bacterium |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0004522 | molecular_function | ribonuclease A activity |
| C | 0004540 | molecular_function | RNA nuclease activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0009617 | biological_process | response to bacterium |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0050830 | biological_process | defense response to Gram-positive bacterium |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0004522 | molecular_function | ribonuclease A activity |
| D | 0004540 | molecular_function | RNA nuclease activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0009617 | biological_process | response to bacterium |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0050830 | biological_process | defense response to Gram-positive bacterium |
| E | 0002181 | biological_process | cytoplasmic translation |
| E | 0005634 | cellular_component | nucleus |
| E | 0005654 | cellular_component | nucleoplasm |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0008428 | molecular_function | ribonuclease inhibitor activity |
| E | 0016477 | biological_process | cell migration |
| E | 0030027 | cellular_component | lamellipodium |
| E | 0032055 | biological_process | negative regulation of translation in response to stress |
| E | 0032311 | cellular_component | angiogenin-PRI complex |
| E | 0034315 | biological_process | regulation of Arp2/3 complex-mediated actin nucleation |
| E | 0036416 | biological_process | tRNA stabilization |
| E | 0045765 | biological_process | regulation of angiogenesis |
| F | 0002181 | biological_process | cytoplasmic translation |
| F | 0005634 | cellular_component | nucleus |
| F | 0005654 | cellular_component | nucleoplasm |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0008428 | molecular_function | ribonuclease inhibitor activity |
| F | 0016477 | biological_process | cell migration |
| F | 0030027 | cellular_component | lamellipodium |
| F | 0032055 | biological_process | negative regulation of translation in response to stress |
| F | 0032311 | cellular_component | angiogenin-PRI complex |
| F | 0034315 | biological_process | regulation of Arp2/3 complex-mediated actin nucleation |
| F | 0036416 | biological_process | tRNA stabilization |
| F | 0045765 | biological_process | regulation of angiogenesis |
| G | 0002181 | biological_process | cytoplasmic translation |
| G | 0005634 | cellular_component | nucleus |
| G | 0005654 | cellular_component | nucleoplasm |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0008428 | molecular_function | ribonuclease inhibitor activity |
| G | 0016477 | biological_process | cell migration |
| G | 0030027 | cellular_component | lamellipodium |
| G | 0032055 | biological_process | negative regulation of translation in response to stress |
| G | 0032311 | cellular_component | angiogenin-PRI complex |
| G | 0034315 | biological_process | regulation of Arp2/3 complex-mediated actin nucleation |
| G | 0036416 | biological_process | tRNA stabilization |
| G | 0045765 | biological_process | regulation of angiogenesis |
| H | 0002181 | biological_process | cytoplasmic translation |
| H | 0005634 | cellular_component | nucleus |
| H | 0005654 | cellular_component | nucleoplasm |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0008428 | molecular_function | ribonuclease inhibitor activity |
| H | 0016477 | biological_process | cell migration |
| H | 0030027 | cellular_component | lamellipodium |
| H | 0032055 | biological_process | negative regulation of translation in response to stress |
| H | 0032311 | cellular_component | angiogenin-PRI complex |
| H | 0034315 | biological_process | regulation of Arp2/3 complex-mediated actin nucleation |
| H | 0036416 | biological_process | tRNA stabilization |
| H | 0045765 | biological_process | regulation of angiogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 126 |
| Chain | Residue |
| A | GLN29 |
| A | HOH631 |
| E | ASN89 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG E 457 |
| Chain | Residue |
| E | LYS269 |
| E | ASP270 |
| E | ARG273 |
| H | GLU94 |
| H | ALA95 |
| H | LEU127 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E 458 |
| Chain | Residue |
| E | SER231 |
| E | ASN232 |
| E | LYS233 |
| E | GLU260 |
| E | ASP262 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO E 459 |
| Chain | Residue |
| E | GLU8 |
| E | GLN9 |
| E | ASP32 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO F 457 |
| Chain | Residue |
| F | SER231 |
| F | ASN232 |
| F | LYS233 |
| F | GLU260 |
| F | ASP262 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO F 458 |
| Chain | Residue |
| B | GLN29 |
| F | ASN89 |
| F | HOH926 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO F 459 |
| Chain | Residue |
| B | ARG33 |
| F | GLN9 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO G 457 |
| Chain | Residue |
| G | SER231 |
| G | ASN232 |
| G | LYS233 |
| G | GLU260 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO G 458 |
| Chain | Residue |
| G | GLU62 |
| G | ASN89 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO G 459 |
| Chain | Residue |
| G | SER383 |
| G | HOH870 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO G 460 |
| Chain | Residue |
| G | CYS7 |
| G | GLN9 |
| G | ASP32 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO H 457 |
| Chain | Residue |
| H | ASN61 |
| H | GLU62 |
| H | ASN89 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO H 458 |
| Chain | Residue |
| H | SER383 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO H 459 |
| Chain | Residue |
| D | ARG33 |
| H | GLN9 |
Functional Information from PROSITE/UniProt
| site_id | PS00127 |
| Number of Residues | 7 |
| Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF |
| Chain | Residue | Details |
| A | CYS41-PHE47 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 108 |
| Details | Repeat: {"description":"LRR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 108 |
| Details | Repeat: {"description":"LRR 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 108 |
| Details | Repeat: {"description":"LRR 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 108 |
| Details | Repeat: {"description":"LRR 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 9"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 108 |
| Details | Repeat: {"description":"LRR 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 11"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 108 |
| Details | Repeat: {"description":"LRR 12"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 13"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 108 |
| Details | Repeat: {"description":"LRR 14"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 112 |
| Details | Repeat: {"description":"LRR 15"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P10775","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13489","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
