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2EIW

Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from Thermus thermophilus with bound L-proline

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
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
B0003842molecular_function1-pyrroline-5-carboxylate dehydrogenase activity
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 ACT A 1520
ChainResidue
AARG462
APHE464
AHIS465
AHOH5833
BVAL172
BLYS510

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1540
ChainResidue
AASP211
AHOH5703
AHOH5916
ASER55
ALEU56
AGLU123

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 5520
ChainResidue
ALYS510
BARG462
BPHE464
BHIS465
BHOH5719

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 5540
ChainResidue
BSER55
BLEU56
BGLU123
BASP211
BHOH5892
BHOH5893

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PRO A 5517
ChainResidue
AGLU137
APHE185
ASER323
AGLY477
AALA478
APHE485
AHOH5552
AHOH5666

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PRO B 5541
ChainResidue
BGLU137
BPHE185
BSER323
BGLY477
BALA478
BPHE485
BHOH5548
BHOH5657

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD B 1530
ChainResidue
AALA148
AHOH5595
BGLU158
BVAL160
BHOH5622
BHOH5644

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 1531
ChainResidue
AASP359
AHOH5635

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 1532
ChainResidue
AGLU241
AGLY244
AALA245
AHOH5765

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 1533
ChainResidue
AGLU416
AHOH5574
AHOH5669

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 5530
ChainResidue
AGLU158
AHOH5602
AHOH5706
BPHE6
BTYR144
BALA148
BHOH5616

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD A 5531
ChainResidue
AARG151

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 5532
ChainResidue
AHOH5777
BARG151
BTYR171
BLEU500

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 5534
ChainResidue
BGLU241
BGLY244
BALA245
BVAL264

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD B 5535
ChainResidue
AARG28
ATYR122
AGLU355
BPRO353
BGLU355
BGLU356
BHOH5704

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD B 5536
ChainResidue
BTYR315
BASP359
BHOH5639

Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YgFQGQKCSAAS
ChainResidueDetails
ATYR315-SER326

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. VETGGKNA
ChainResidueDetails
AVAL287-ALA294

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PDB entries from 2024-06-12

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