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4Q72

Crystal Structure of Bradyrhizobium japonicum Proline Utilization A (PutA) Mutant D779Y

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
A0042802molecular_functionidentical protein binding
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
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD A 2001
ChainResidue
AASP278
AALA344
ATYR345
ATRP346
APHE364
ATHR365
AARG366
ALYS367
ATHR370
AALA393
ATHR394
AALA279
AHIS395
AASN396
ATYR441
ASER466
APHE467
AHOH2120
AHOH2149
AHOH2190
AALA310
AGLN312
ATYR314
AARG339
AVAL341
ALYS342
AGLY343

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 2002
ChainResidue
ASER30
APRO32
AARG36

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 2003
ChainResidue
AGLU256
AALA297
APRO299
ALYS302
AHIS332
AARG334
AHOH2283

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 2004
ChainResidue
AASP359
AVAL517
AGLU518
AALA524
AHOH2239

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 2005
ChainResidue
AARG475
AARG475

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2006
ChainResidue
AARG366
ALYS367
AALA368
AHOH2124

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2007
ChainResidue
AARG791
ASER793
AILE945
AGLY946
AALA947
AHOH2152

site_idAC8
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD B 1001
ChainResidue
BASP278
BALA279
BALA310
BGLN312
BTYR314
BARG339
BVAL341
BLYS342
BGLY343
BALA344
BTRP346
BPHE364
BTHR365
BARG366
BLYS367
BTHR370
BALA393
BTHR394
BHIS395
BASN396
BTYR441
BSER466
BPHE467
BHOH1131

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1002
ChainResidue
BPHE659
BARG791
BSER793
BILE945
BGLY946
BALA947

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1003
ChainResidue
BARG475
BARG475

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1004
ChainResidue
BARG366
BLYS367
BALA368
BHOH1145

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FrSAGQRCSALR
ChainResidueDetails
APHE785-ARG796

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. IAATlaDpSLKGWDG
ChainResidueDetails
AILE292-GLY306

221051

PDB entries from 2024-06-12

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