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5N6C

Crystal structure of human 3-phosphoglycerate dehydrogenase in complex with NAD and L-Tartrate

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 Residues11
Detailsbinding site for residue TLA A 401
ChainResidue
AARG54
AHOH514
BARG135
ASER55
AARG75
ATHR78
AARG236
AHIS283
AALA286
AGLN292
ANAD402

site_idAC2
Number of Residues26
Detailsbinding site for residue NAD A 402
ChainResidue
ATHR78
AASN102
AGLY152
AGLY154
AARG155
AILE156
ATYR174
AASP175
APRO176
AILE177
AHIS206
ATHR207
APRO208
ATHR213
ACYS234
AALA235
AARG236
AASP260
AHIS283
AGLY285
AALA286
ATLA401
AHOH505
AHOH509
AHOH520
AHOH524

site_idAC3
Number of Residues21
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY152
BGLY154
BARG155
BILE156
BTYR174
BASP175
BPRO176
BILE177
BHIS206
BTHR207
BPRO208
BTHR213
BCYS234
BALA235
BARG236
BASP260
BHIS283
BGLY285
BALA286
BHOH503
BHOH514

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
ALEU148-ASP175

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. IWplCDFItVHtPllpsTtgLlN
ChainResidueDetails
AILE196-ASN218

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. CKkGvRVVNcARGgIVD
ChainResidueDetails
ACYS225-ASP241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AARG236
BARG236

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
BGLU265
AGLU265

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS283
BHIS283

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|Ref.21
ChainResidueDetails
AASP175
ATHR207
ACYS234
AASP260
AHIS283
BTHR78
BARG155
BASP175
BTHR207
BCYS234
BASP260
BHIS283
ATHR78
AARG155

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER14
BSER14

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q61753
ChainResidueDetails
ALYS21
BLYS21

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61753
ChainResidueDetails
ALYS58
BLYS58

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR78
BTHR78

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
BLYS21
ALYS21

221051

PDB entries from 2024-06-12

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