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3QRD

Crystal structure of L68V mutant of human cystatin C

Functional Information from GO Data
ChainGOidnamespacecontents
A0001540molecular_functionamyloid-beta binding
A0002020molecular_functionprotease binding
A0004866molecular_functionendopeptidase inhibitor activity
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006952biological_processdefense response
A0010466biological_processnegative regulation of peptidase activity
A0010711biological_processnegative regulation of collagen catabolic process
A0010716biological_processnegative regulation of extracellular matrix disassembly
A0030414molecular_functionpeptidase inhibitor activity
A0031982cellular_componentvesicle
A0034103biological_processregulation of tissue remodeling
A0042802molecular_functionidentical protein binding
A0045861biological_processnegative regulation of proteolysis
A0060311biological_processnegative regulation of elastin catabolic process
A0060313biological_processnegative regulation of blood vessel remodeling
A0070062cellular_componentextracellular exosome
A0097435biological_processsupramolecular fiber organization
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0001540molecular_functionamyloid-beta binding
B0002020molecular_functionprotease binding
B0004866molecular_functionendopeptidase inhibitor activity
B0004869molecular_functioncysteine-type endopeptidase inhibitor activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0006952biological_processdefense response
B0010466biological_processnegative regulation of peptidase activity
B0010711biological_processnegative regulation of collagen catabolic process
B0010716biological_processnegative regulation of extracellular matrix disassembly
B0030414molecular_functionpeptidase inhibitor activity
B0031982cellular_componentvesicle
B0034103biological_processregulation of tissue remodeling
B0042802molecular_functionidentical protein binding
B0045861biological_processnegative regulation of proteolysis
B0060311biological_processnegative regulation of elastin catabolic process
B0060313biological_processnegative regulation of blood vessel remodeling
B0070062cellular_componentextracellular exosome
B0097435biological_processsupramolecular fiber organization
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
C0001540molecular_functionamyloid-beta binding
C0002020molecular_functionprotease binding
C0004866molecular_functionendopeptidase inhibitor activity
C0004869molecular_functioncysteine-type endopeptidase inhibitor activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005788cellular_componentendoplasmic reticulum lumen
C0005794cellular_componentGolgi apparatus
C0005886cellular_componentplasma membrane
C0006952biological_processdefense response
C0010466biological_processnegative regulation of peptidase activity
C0010711biological_processnegative regulation of collagen catabolic process
C0010716biological_processnegative regulation of extracellular matrix disassembly
C0030414molecular_functionpeptidase inhibitor activity
C0031982cellular_componentvesicle
C0034103biological_processregulation of tissue remodeling
C0042802molecular_functionidentical protein binding
C0045861biological_processnegative regulation of proteolysis
C0060311biological_processnegative regulation of elastin catabolic process
C0060313biological_processnegative regulation of blood vessel remodeling
C0070062cellular_componentextracellular exosome
C0097435biological_processsupramolecular fiber organization
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
D0001540molecular_functionamyloid-beta binding
D0002020molecular_functionprotease binding
D0004866molecular_functionendopeptidase inhibitor activity
D0004869molecular_functioncysteine-type endopeptidase inhibitor activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005788cellular_componentendoplasmic reticulum lumen
D0005794cellular_componentGolgi apparatus
D0005886cellular_componentplasma membrane
D0006952biological_processdefense response
D0010466biological_processnegative regulation of peptidase activity
D0010711biological_processnegative regulation of collagen catabolic process
D0010716biological_processnegative regulation of extracellular matrix disassembly
D0030414molecular_functionpeptidase inhibitor activity
D0031982cellular_componentvesicle
D0034103biological_processregulation of tissue remodeling
D0042802molecular_functionidentical protein binding
D0045861biological_processnegative regulation of proteolysis
D0060311biological_processnegative regulation of elastin catabolic process
D0060313biological_processnegative regulation of blood vessel remodeling
D0070062cellular_componentextracellular exosome
D0097435biological_processsupramolecular fiber organization
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 121
ChainResidue
AALA46
ALEU47
AASN82
AHOH141
BARG45

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 122
ChainResidue
AGLN100
ALYS114
AHOH139

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG D 121
ChainResidue
DASN79
DASN82
DCYS83
DPRO84
DHOH136
DHOH139
DCYS73

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG D 122
ChainResidue
CASN61
CTYR102
DASN61
DHOH135

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG D 123
ChainResidue
ASER115
BALA37
DGLN118

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG D 124
ChainResidue
AARG25
DPRO78
DASN79
DLEU80

Functional Information from PROSITE/UniProt
site_idPS00287
Number of Residues14
DetailsCYSTATIN Cysteine proteases inhibitors signature. KQIVAGVNYfLDVE
ChainResidueDetails
ALYS54-GLU67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Reactive site
ChainResidueDetails
AGLY11
BGLY11
CGLY11
DGLY11

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER17
BSER17
CSER17
DSER17

227344

PDB entries from 2024-11-13

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