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2ULL

MULTIPLE CONFORMATION STRUCTURE OF ALPHA-LYTIC PROTEASE AT 120 K

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AARG48
AHOH499
AGLN237
ATYR238
AHOH272
AHOH273
AHOH274
AHOH440
AHOH441
AHOH442

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AALA15
AASN15
AARG230
APRO233
AHOH248
AHOH323
AHOH400
AHOH401
AHOH460
AHOH462

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
AHIS57
AARG122
AGLY193
ASER195
AHOH406
AHOH421
AHOH422
AHOH423
AHOH544

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TAM A 1
ChainResidue
AHIS57
AARG122
ATYR171
AGLU174
ASER214
AGLY215
AHOH339
AHOH340
AHOH341
AHOH342
AHOH407
AHOH504

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. CMgrGDSGGSWI
ChainResidueDetails
ACYS189-ILE200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
AHIS57
AASP102
ASER195

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57
ASER214

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idMCSA1
Number of Residues5
DetailsM-CSA 609
ChainResidueDetails
AHIS57proton acceptor, proton donor
AASP102electrostatic stabiliser
AGLY193electrostatic stabiliser
ASER195electrostatic stabiliser
ASER214electrostatic stabiliser

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PDB entries from 2024-11-06

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