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

1THM

CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AASP5
AASP47
AVAL82
AASN85
ATHR87
AILE89

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AASP57
AASP62
ATHR64
AGLN66
AHOH353
AHOH370

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 303
ChainResidue
AALA173
ATYR175
AALA178
AASP201
AHOH335
AHOH420

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
ASER191
ASER192
APHE193
ASER207
AHOH416

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
AGLN144
ATYR175
ASER176
AHOH320
AHOH350

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 306
ChainResidue
APHE8
ASER9
AGLN16
AASN140
ASER141
AHOH455

site_idACT
Number of Residues3
DetailsENZYME CATALYTIC SITE
ChainResidue
AASP38
AHIS71
ASER225

site_idIO1
Number of Residues6
DetailsION BINDING SITE 1
ChainResidue
AASP5
AASP47
AVAL82
AASN85
ATHR87
AILE89

site_idIO2
Number of Residues6
DetailsION BINDING SITE 2
ChainResidue
AASP57
AASP62
ATHR64
AGLN66
AHOH353
AHOH370

site_idIO3
Number of Residues6
DetailsION BINDING SITE 3
ChainResidue
AALA173
ATYR175
AALA178
AASP201
AHOH335
AHOH420

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. IAIVDTGVqsnH
ChainResidueDetails
AILE34-HIS45

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThCAGiAAA
ChainResidueDetails
AHIS71-ALA81

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG
ChainResidueDetails
AGLY223-GLY233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP38
AHIS71
ASER225

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:1993669, ECO:0000269|PubMed:2688688, ECO:0007744|PDB:1TEC, ECO:0007744|PDB:3TEC
ChainResidueDetails
AASP5
ATHR87
AILE89
AASP47
AASP57
AASP60
AASP62
ATHR64
AGLN66
AVAL82
AASN85

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:2688688, ECO:0007744|PDB:1TEC
ChainResidueDetails
AALA173
ATYR175
AALA178
AASP201

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:1993669, ECO:0007744|PDB:3TEC
ChainResidueDetails
ATRP199

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
AASP38
AHIS71
ASER225

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon