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5CH8

Crystal structure of MDLA N225Q mutant form Penicillium cyclopium

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0017000biological_processantibiotic biosynthetic process
A0046872molecular_functionmetal ion binding
A0072330biological_processmonocarboxylic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AGLU129
AASP237
AASP239
AHOH606

site_idAC2
Number of Residues3
Detailsbinding site for residue ZN A 302
ChainResidue
AASP8
AGLU43
AHOH408

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 303
ChainResidue
AHOH528
APHE12
AASN73

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 304
ChainResidue
ATYR21
ASER145

site_idAC5
Number of Residues4
Detailsbinding site for residue CL A 305
ChainResidue
ATHR197
AASN224
AHOH421
AHOH552

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 306
ChainResidue
ASER58
AILE60
ATHR61
AHOH409

site_idAC7
Number of Residues3
Detailsbinding site for residue CL A 307
ChainResidue
ALYS33
AASP104
AHOH585

site_idAC8
Number of Residues11
Detailsbinding site for residue GOL A 308
ChainResidue
AASP62
ATHR63
AGLY82
ASER83
AGLY111
APHE112
ASER115
ALEU146
AVAL150
AHOH461
AHOH468

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LVVVGHSLGA
ChainResidueDetails
ALEU139-ALA148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|DOI:10.1002/slct.201600254
ChainResidueDetails
ASER145

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:P61870
ChainResidueDetails
AASP199

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|DOI:10.1002/slct.201600254
ChainResidueDetails
AHIS259

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|DOI:10.1002/slct.201600254, ECO:0007744|PDB:5CH8
ChainResidueDetails
AASP237
AASP239

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AGLN225

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PDB entries from 2024-07-24

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