Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7MY9

Structure of proline utilization A with 1,3-dithiolane-2-carboxylate bound in the proline 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 Residues6
Detailsbinding site for residue UJD A 1301
ChainResidue
ALYS265
ATYR473
ATYR485
AARG488
AARG489
AFAD1302

site_idAC2
Number of Residues36
Detailsbinding site for residue FAD A 1302
ChainResidue
AGLN340
ATYR342
AARG367
AVAL369
ALYS370
AGLY371
AALA372
ATYR373
ATRP374
APHE392
ATHR393
AARG394
ALYS395
ATHR398
AALA421
ATHR422
AHIS423
AASN424
ACYS448
ALEU449
ATYR473
AARG489
AGLU492
ASER497
ASER498
APHE499
AILE1232
AGLY1233
AUJD1301
AHOH1424
AHOH1430
AHOH1465
AHOH1966
AASP306
AALA307
AVAL338

site_idAC3
Number of Residues33
Detailsbinding site for residue NAD A 1303
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
AMG1307
AHOH1402
AHOH1460
AHOH1528
AHOH1696
AHOH1786
AHOH1949
AHOH2035
AHOH2081

site_idAC4
Number of Residues10
Detailsbinding site for residue SO4 A 1304
ChainResidue
AARG688
APRO1039
AGLN1040
AHOH1521
AHOH1564
AHOH2048
AHOH2065
BSER94
BGLN96
BARG170

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 1305
ChainResidue
ASER1194
AGLY1196
AARG1200
AHOH1420

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 1306
ChainResidue
ALYS1060
ALYS1139
AHOH1410

site_idAC7
Number of Residues6
Detailsbinding site for residue MG A 1307
ChainResidue
ANAD1303
AHOH1460
AHOH1650
AHOH1696
AHOH2081
BHOH2227

site_idAC8
Number of Residues5
Detailsbinding site for residue PGE A 1308
ChainResidue
AGLY1079
ALEU1096
AHIS1097
AHOH1819
AHIS1045

site_idAC9
Number of Residues6
Detailsbinding site for residue UJD B 1301
ChainResidue
BASP306
BTYR473
BTYR485
BARG488
BARG489
BFAD1303

site_idAD1
Number of Residues6
Detailsbinding site for residue PEG B 1302
ChainResidue
BGLU674
BPHE708
BALA711
BILE712
BHOH1775
BHOH2156

site_idAD2
Number of Residues32
Detailsbinding site for residue FAD B 1303
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
BARG489
BGLU492
BSER498
BPHE499
BUJD1301
BHOH1506
BHOH1531
BHOH2022

site_idAD3
Number of Residues32
Detailsbinding site for residue NAD B 1304
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
BMG1306
BHOH1402
BHOH1480
BHOH1611
BHOH1615
BHOH1818
BHOH1894
BHOH2064

site_idAD4
Number of Residues8
Detailsbinding site for residue SO4 B 1305
ChainResidue
ASER94
AARG170
BARG688
BPRO1039
BGLN1040
BHOH1575
BHOH1608
BHOH1685

site_idAD5
Number of Residues6
Detailsbinding site for residue MG B 1306
ChainResidue
BNAD1304
BHOH1615
BHOH1818
BHOH1894
BHOH2064
BHOH2315

site_idAD6
Number of Residues5
Detailsbinding site for residue PGE B 1307
ChainResidue
BHIS1045
BGLY1079
BHIS1097
BHOH1643
BHOH1814

site_idAD7
Number of Residues6
Detailsbinding site for residue PGE B 1308
ChainResidue
BALA581
BTHR582
BHOH1481
BHOH1800
BHOH2155
BHOH2192

site_idAD8
Number of Residues8
Detailsbinding site for residue PG4 B 1309
ChainResidue
AMET434
AGLY436
AHOH1507
BASN894
BLYS897
BARG939
BHOH1440
BHOH2167

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon