Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KLT

CRYSTAL STRUCTURE OF PMSF-TREATED HUMAN CHYMASE AT 1.9 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0002003biological_processangiotensin maturation
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0008236molecular_functionserine-type peptidase activity
A0016485biological_processprotein processing
A0022617biological_processextracellular matrix disassembly
A0030141cellular_componentsecretory granule
A0030163biological_processprotein catabolic process
A0030901biological_processmidbrain development
A0034769biological_processbasement membrane disassembly
A0036464cellular_componentcytoplasmic ribonucleoprotein granule
A0042277molecular_functionpeptide binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0045766biological_processpositive regulation of angiogenesis
A0050727biological_processregulation of inflammatory response
A0062023cellular_componentcollagen-containing extracellular matrix
A0071333biological_processcellular response to glucose stimulus
A0140447biological_processcytokine precursor processing
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PMS A 400
ChainResidue
AHOH522
AHIS57
APHE191
ALYS192
AGLY193
ASER195
ASER214

site_idCIC
Number of Residues3
DetailsACTIVE SITE
ChainResidue
AASP102
AHIS57
ASER195

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SAfkGDSGGPLL
ChainResidueDetails
ASER189-LEU200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2071582
ChainResidueDetails
AASN72

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN95

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY196

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY193

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
AHIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon