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

3C17

Hexagonal Crystal Structure of Precursor E. coli Isoaspartyl Peptidase/l-Asparaginase (ECAIII) with Active-site T179A mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004067molecular_functionasparaginase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008798molecular_functionbeta-aspartyl-peptidase activity
A0016540biological_processprotein autoprocessing
A0016787molecular_functionhydrolase activity
B0004067molecular_functionasparaginase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008798molecular_functionbeta-aspartyl-peptidase activity
B0016540biological_processprotein autoprocessing
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1
ChainResidue
ALEU60
AGLU61
ACYS63
APHE66
AALA68
AILE70

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 322
ChainResidue
BPHE66
BALA68
BILE70
BLEU60
BGLU61
BCYS63

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 322
ChainResidue
APHE290
ATHR292
AHOH459
AHOH528
AHOH529

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 323
ChainResidue
AHOH448
BHOH388
BHOH389
BHOH390
BHOH491
BHOH493

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 323
ChainResidue
AMET114
ASER117
AHIS119
AHOH412
AHOH426

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 324
ChainResidue
BMET114
BSER117
BHIS119
BHOH383
BHOH443

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 324
ChainResidue
ALYS176
AGLY231
AHOH374
AHOH375

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 325
ChainResidue
BLYS176
BGLY231
BHOH370
BHOH378

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 326
ChainResidue
BALA155
BALA156
BLYS158
BGLY160
BHOH520

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 327
ChainResidue
BPHE290
BTHR292
BHOH496
BHOH497
BHOH499

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 325
ChainResidue
AHOH535
AHOH536
AHOH537
AHOH538
BHOH442
BHOH512

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 326
ChainResidue
AHOH440
BLEU92
BHOH390
BHOH454

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 328
ChainResidue
BMET136
BGLU137

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 327
ChainResidue
AARG17
AALA18

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 329
ChainResidue
ATYR311
BSER21
BLEU22
BHOH519

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 330
ChainResidue
BARG17
BALA18

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 328
ChainResidue
AILE310
ATYR311
BGLN23
BHOH519

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 331
ChainResidue
BALA14
BTHR292
BGLU293

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 329
ChainResidue
AALA14
AGLU293
AHOH405
AHOH481

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 330
ChainResidue
AARG207
AGLY231
AGLY233

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 332
ChainResidue
BARG207
BGLY231
BGLY233
BHOH379

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 331
ChainResidue
AARG238
AHOH347
BHOH443

site_idCC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 333
ChainResidue
AHOH426
BARG238

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 334
ChainResidue
AHOH535
BARG262
BLYS267

site_idCC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 332
ChainResidue
BTYR311
AGLN23
BILE310

site_idCC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 335
ChainResidue
ASER21
ALEU22
AHOH507
BARG17
BTYR311

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 333
ChainResidue
AARG262
ALYS267
BHOH494

site_idDC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 334
ChainResidue
AMET136
AGLU137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:18323626
ChainResidueDetails
AALA179
BALA179

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15946951, ECO:0007744|PDB:2ZAL
ChainResidueDetails
AARG207
ATHR230
BARG207
BTHR230

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:11988085
ChainResidueDetails
AGLY178
BGLY178

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
AASN67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
BASN67

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
AGLY69

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1apy
ChainResidueDetails
BGLY69

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon