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5MLN

The crystal structure of alcohol dehydrogenase 10 from Candida magnoliae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue NAP A 301
ChainResidue
AGLY11
AASP63
ALEU64
AASN89
AALA90
AGLY91
AVAL112
AILE142
ASER143
ASER144
ATYR157
ASER13
ALYS161
APRO187
AGLY188
ATYR189
ATHR190
ATHR192
AMET194
ATHR195
AHOH418
AHOH434
AARG14
AHOH436
AHOH462
AHOH481
AGLY15
AILE16
ASER35
AARG36
ASER37
ALEU62

site_idAC2
Number of Residues3
Detailsbinding site for residue PEG A 302
ChainResidue
AASP217
ALEU220
BLYS224

site_idAC3
Number of Residues5
Detailsbinding site for residue PEG A 303
ChainResidue
ASER5
AASN6
AHOH404
AHOH405
BGLU199

site_idAC4
Number of Residues3
Detailsbinding site for residue PEG A 304
ChainResidue
AHOH403
AHOH452
BVAL234

site_idAC5
Number of Residues33
Detailsbinding site for residue NAP B 301
ChainResidue
BGLY11
BSER13
BARG14
BGLY15
BILE16
BSER35
BARG36
BSER37
BLEU62
BASP63
BLEU64
BALA65
BASN89
BALA90
BGLY91
BILE142
BSER143
BSER144
BTYR157
BLYS161
BPRO187
BGLY188
BTYR189
BTHR190
BTHR192
BGLU193
BMET194
BTHR195
BHOH414
BHOH427
BHOH438
BHOH439
BHOH445

site_idAC6
Number of Residues5
Detailsbinding site for residue PEG B 302
ChainResidue
ALEU148
AARG169
BLEU148
BHOH444
BHOH521

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvaglhgaaqVavYSASKAGLdGFMrSVA
ChainResidueDetails
ASER144-ALA172

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PDB entries from 2024-09-11

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