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2O2R

Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 2001
ChainResidue
ALYS852
CARG554
CHOH3216

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AARG554
AHOH3029
CLYS852

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2003
ChainResidue
BARG554
DLYS852
DHOH3123

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 2004
ChainResidue
BLYS852
DARG554
DHOH3036

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2005
ChainResidue
BARG636
BPRO641
BHOH3174

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 2006
ChainResidue
AARG636

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 2007
ChainResidue
CARG636
CPRO641

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 2008
ChainResidue
DARG636
DPRO641

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 2009
ChainResidue
BARG764
BTYR799

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 C 2010
ChainResidue
CARG764

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 2011
ChainResidue
AARG764

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 D 2012
ChainResidue
DARG764

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 2013
ChainResidue
CLYS669
CLEU893
CARG894
CILE895
CHOH3192
DGLY881
DLYS882
DHOH3066

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 2014
ChainResidue
AGLY881
ALYS882
BLYS669
BLEU893
BARG894
BILE895
BHOH3004
BHOH3175

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 2015
ChainResidue
ALYS669
ALEU893
AARG894
AILE895
AHOH3159
AHOH3174
BGLY881
BLYS882
BHOH3019

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 D 2016
ChainResidue
CGLY881
CLYS882
DLYS669
DLEU893
DARG894
DILE895
DHOH3007
DHOH3160
DHOH3214

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 2017
ChainResidue
ALEU416
ATHR417
CLYS415
CARG742

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 2018
ChainResidue
ATYR848
CARG551
CARG554

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2019
ChainResidue
AARG551
AARG554
CTYR848

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2020
ChainResidue
BARG551
BARG554
DTYR848

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 2021
ChainResidue
BTYR848
DARG551
DARG554

site_idCC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NDP A 903
ChainResidue
AVAL570
AILE571
ATRP573
ALYS597
AALA599
AGLN600
ASER629
AGLY630
AGLY634
AGLN635
APHE648
ATHR649
ASER651
AVAL654
AHIS657
AILE658
AHOH3027
AHOH3046
AHOH3047
AHOH3074
AHOH3109

site_idCC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NDP B 903
ChainResidue
BLYS597
BALA599
BGLN600
BSER629
BGLY630
BGLY634
BGLN635
BPHE648
BTHR649
BGLY650
BSER651
BVAL654
BHIS657
BILE658
BHOH3023
BHOH3083
BHOH3110
BHOH3137
BHOH3144
BVAL570
BILE571
BTRP573

site_idCC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NDP C 903
ChainResidue
CVAL570
CILE571
CTRP573
CLYS597
CALA599
CGLN600
CSER629
CGLY630
CGLY634
CGLN635
CPHE648
CTHR649
CSER651
CVAL654
CHIS657
CILE658
CHOH3043
CHOH3044
CHOH3053
CHOH3058
CHOH3139

site_idCC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NDP D 903
ChainResidue
DVAL570
DILE571
DTRP573
DLYS597
DALA599
DGLN600
DSER629
DGLY630
DGLY634
DGLN635
DPHE648
DSER651
DVAL654
DHIS657
DILE658
DHOH3030
DHOH3042
DHOH3062
DHOH3081
DHOH3146
DHOH3180

site_idCC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 3001
ChainResidue
ATYR575
AMET578
AASN706
ACYS707
AILE708
ATHR866

site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 3002
ChainResidue
BMET578
BASN706
BASN864
BTHR866

site_idDC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 3003
ChainResidue
CTYR575
CMET578
CASN706
CASN864
CTHR866

site_idDC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 3004
ChainResidue
DTYR575
DMET578
DASN706
DASN864
DTHR866

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNKGENCIAAG
ChainResidueDetails
APHE700-GLY711

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU672-PRO679

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17302434
ChainResidueDetails
AGLU673
BGLU673
CGLU673
DGLU673

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:17302434, ECO:0000305|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:3RHO
ChainResidueDetails
ACYS707
BCYS707
CCYS707
DCYS707

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR
ChainResidueDetails
BILE571
BLYS597
BGLY630
BGLY650
CILE571
CLYS597
CGLY630
CGLY650
DILE571
DLYS597
DGLY630
DGLY650
AILE571
ALYS597
AGLY630
AGLY650

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR
ChainResidueDetails
CGLU673
CGLU804
DGLU673
DGLU804
AGLU673
AGLU804
BGLU673
BGLU804

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21540484, ECO:0007744|PDB:3RHO
ChainResidueDetails
ALYS757
BLYS757
CLYS757
DLYS757

site_idSWS_FT_FI6
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O75891
ChainResidueDetails
BSER631
BSER825
CSER629
CSER631
CSER825
DSER629
DSER631
DSER825
ASER629
ASER631
ASER825
BSER629

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K009
ChainResidueDetails
ALYS660
BLYS660
CLYS660
DLYS660

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R0Y6
ChainResidueDetails
ALYS767
BLYS767
CLYS767
DLYS767

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q3SY69
ChainResidueDetails
ALYS882
BLYS882
CLYS882
DLYS882

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
ACYS707

site_idMCSA2
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
BCYS707

site_idMCSA3
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
CCYS707

site_idMCSA4
Number of Residues1
DetailsM-CSA 766
ChainResidueDetails
DCYS707

220472

PDB entries from 2024-05-29

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