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5C1C

Crystal Structure of the Pectin Methylesterase from Aspergillus niger in Deglycosylated Form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0030599molecular_functionpectinesterase activity
A0042545biological_processcell wall modification
A0045490biological_processpectin catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 A 401
ChainResidue
ATYR178
ATRP198
AGLY200
ALYS311
AHOH590
AHOH603
AHOH627

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
AGOL407
AHOH572
AHOH624
ATRP251
AARG252

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 403
ChainResidue
AASP222
ASER223
AARG256
AHOH647

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 404
ChainResidue
ALYS98
ATHR219
ASER220
ASER221
AHOH545
AHOH582

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 405
ChainResidue
APRO111
AGLU218
AARG252
AHOH666

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 406
ChainResidue
AASN152
ALYS173

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL A 407
ChainResidue
AGLN145
AASP168
AASP189
ATRP251
AMET276
ASO4402
AHOH662

site_idAC8
Number of Residues9
Detailsbinding site for residue GOL A 408
ChainResidue
ATHR312
AGLU317
AGLU317
ATRP319
ATRP319
AGLY320
AGLY320
AHOH511
AHOH511

site_idAC9
Number of Residues1
Detailsbinding site for residue GOL A 409
ChainResidue
AGLY291

site_idAD1
Number of Residues3
Detailsbinding site for residue ACT A 410
ChainResidue
AARG249
AARG249
AHOH725

Functional Information from PROSITE/UniProt
site_idPS00503
Number of Residues10
DetailsPECTINESTERASE_2 Pectinesterase signature 2. IeGAVDYIFG
ChainResidueDetails
AILE184-GLY193

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PDB entries from 2025-06-18

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