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6X9B

Structure of proline utilization A with cis-4-hydroxy-D-proline bound in the L-glutamate-gamma-semialdehyde dehydrogenase active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003677molecular_functionDNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
A0004657molecular_functionproline dehydrogenase activity
A0006355biological_processregulation of DNA-templated transcription
A0006560biological_processproline metabolic process
A0006561biological_processproline biosynthetic process
A0006562biological_processproline catabolic process
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010133biological_processproline catabolic process to glutamate
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0000166molecular_functionnucleotide binding
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
B0004657molecular_functionproline dehydrogenase activity
B0006355biological_processregulation of DNA-templated transcription
B0006560biological_processproline metabolic process
B0006561biological_processproline biosynthetic process
B0006562biological_processproline catabolic process
B0009898cellular_componentcytoplasmic side of plasma membrane
B0010133biological_processproline catabolic process to glutamate
B0016491molecular_functionoxidoreductase activity
B0016620molecular_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 Residues36
Detailsbinding site for residue FAD A 2001
ChainResidue
AASP306
AALA372
ATYR373
ATRP374
APHE392
ATHR393
AARG394
ALYS395
ATHR398
AALA421
ATHR422
AALA307
AHIS423
AASN424
AGLN447
ACYS448
ALEU449
ATYR473
AGLU492
AASN493
ASER497
ASER498
AVAL338
APHE499
AILE1232
AGLY1233
AHOH2290
AHOH2558
AHOH2742
AHOH2822
AGLN340
ATYR342
AARG367
AVAL369
ALYS370
AGLY371

site_idAC2
Number of Residues5
Detailsbinding site for residue PEG A 2002
ChainResidue
AGLY1079
AASP1081
ALEU1096
AHOH2129
AHOH2607

site_idAC3
Number of Residues36
Detailsbinding site for residue NAD A 2003
ChainResidue
AILE703
ASER704
APRO705
ATRP706
AASN707
AILE712
ALYS730
AALA732
AGLU733
AGLY763
AGLY766
AALA767
APHE780
ATHR781
AGLY782
ASER783
AVAL786
AGLU810
ATHR811
AGLY812
ACYS844
AGLU940
APHE942
APHE1010
AMG2005
AHOH2103
AHOH2336
AHOH2399
AHOH2426
AHOH2711
AHOH2774
AHOH2797
AHOH2807
BHOH2164
BHOH2332
BHOH2474

site_idAC4
Number of Residues10
Detailsbinding site for residue SO4 A 2004
ChainResidue
AARG688
APRO1039
AGLN1040
AHOH2202
AHOH2279
AHOH2608
AHOH2768
BSER94
BGLN96
BARG170

site_idAC5
Number of Residues4
Detailsbinding site for residue MG A 2005
ChainResidue
ANAD2003
AHOH2103
AHOH2797
BHOH2332

site_idAC6
Number of Residues10
Detailsbinding site for residue UYA A 2006
ChainResidue
AHOH2199
AHOH2329
AGLU674
APHE708
AARG843
ACYS844
ASER845
AGLY1002
AALA1003
APHE1010

site_idAC7
Number of Residues31
Detailsbinding site for residue FAD B 2001
ChainResidue
BASP306
BALA307
BVAL338
BGLN340
BTYR342
BARG367
BVAL369
BLYS370
BGLY371
BALA372
BTYR373
BTRP374
BPHE392
BTHR393
BARG394
BLYS395
BTHR398
BALA421
BTHR422
BHIS423
BASN424
BCYS448
BLEU449
BTYR473
BGLU492
BASN493
BSER498
BPHE499
BILE1232
BGLY1233
BHOH2333

site_idAC8
Number of Residues5
Detailsbinding site for residue PGE B 2002
ChainResidue
BHIS1045
BGLY1079
BLEU1096
BHIS1097
BHOH2350

site_idAC9
Number of Residues29
Detailsbinding site for residue NAD B 2003
ChainResidue
BILE703
BSER704
BPRO705
BTRP706
BASN707
BILE712
BLYS730
BALA732
BGLU733
BGLY763
BGLY766
BALA767
BPHE780
BTHR781
BGLY782
BSER783
BVAL786
BGLU810
BTHR811
BGLY812
BCYS844
BGLU940
BPHE942
BPHE1010
BHOH2154
BHOH2252
BHOH2384
BHOH2451
BHOH2629

site_idAD1
Number of Residues8
Detailsbinding site for residue SO4 B 2004
ChainResidue
ASER94
AARG170
BARG688
BPRO1039
BGLN1040
BHOH2238
BHOH2377
BHOH2663

site_idAD2
Number of Residues10
Detailsbinding site for residue UYA B 2005
ChainResidue
BGLU674
BPHE708
BARG843
BCYS844
BSER845
BGLY1002
BALA1003
BPHE1010
BHOH2258
BHOH2567

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FdSAGQRCSALR
ChainResidueDetails
APHE837-ARG848

221051

PDB entries from 2024-06-12

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