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2G76

Crystal structure of human 3-phosphoglycerate dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MLT A 503
ChainResidue
AARG53
AHOH511
AHOH534
BARG134
ASER54
AARG74
ATHR77
AASN101
AARG235
AHIS282
AALA285
ANAD501

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MLT B 504
ChainResidue
AARG134
BARG53
BSER54
BARG74
BTHR77
BASN101
BARG235
BHIS282
BALA285
BNAD502
BHOH519
BHOH576

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD A 501
ChainResidue
ATHR77
AGLY151
AGLY153
AARG154
AILE155
ATYR173
AASP174
APRO175
AHIS205
ATHR206
APRO207
ASER211
ATHR212
ACYS233
AALA234
AARG235
AASP259
AHIS282
AGLY284
AALA285
AMLT503
AHOH516
AHOH535
AHOH550
AHOH554
AHOH555
AHOH576
AHOH590

site_idAC4
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NAD B 502
ChainResidue
AGLU193
BTHR77
BASN101
BALA105
BGLY151
BGLY153
BARG154
BILE155
BTYR173
BASP174
BPRO175
BILE176
BHIS205
BTHR206
BPRO207
BTHR212
BCYS233
BALA234
BARG235
BASP259
BHIS282
BGLY284
BALA285
BMLT504
BHOH526
BHOH557
BHOH561
BHOH570
BHOH580
BHOH582
BHOH592
BHOH602
BHOH618

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGILGlGRIGrevatrmqsfgmk.TIgYD
ChainResidueDetails
ALEU147-ASP174

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. IWplCDFItVHtPllpsTtgLlN
ChainResidueDetails
AILE195-ASN217

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. CKkGvRVVNcARGgIVD
ChainResidueDetails
ACYS224-ASP240

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AGLY236
BGLY236

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
APRO265
BPRO265

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ALEU283
BLEU283

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|Ref.21
ChainResidueDetails
AGLY78
BPRO175
BPRO207
BALA234
BVAL260
BLEU283
AILE155
APRO175
APRO207
AALA234
AVAL260
ALEU283
BGLY78
BILE155

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ALEU14
BLEU14

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q61753
ChainResidueDetails
AILE21
BILE21

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61753
ChainResidueDetails
AVAL58
BVAL58

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLY78
BGLY78

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
AILE21
BILE21

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
AGLU264
AASP259
AGLY237
AHIS282
AARG235

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
BGLU264
BASP259
BGLY237
BHIS282
BARG235

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
AGLU264
AHIS282

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gdh
ChainResidueDetails
BGLU264
BHIS282

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PDB entries from 2024-07-17

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