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2CWH

Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006560biological_processproline metabolic process
A0016491molecular_functionoxidoreductase activity
A0030416biological_processmethylamine metabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0047125molecular_functiondelta1-piperideine-2-carboxylate reductase activity
A0050132molecular_functionN-methylalanine dehydrogenase activity
A0050241molecular_functionpyrroline-2-carboxylate reductase activity
A0070401molecular_functionNADP+ binding
B0000166molecular_functionnucleotide binding
B0006560biological_processproline metabolic process
B0016491molecular_functionoxidoreductase activity
B0030416biological_processmethylamine metabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0047125molecular_functiondelta1-piperideine-2-carboxylate reductase activity
B0050132molecular_functionN-methylalanine dehydrogenase activity
B0050241molecular_functionpyrroline-2-carboxylate reductase activity
B0070401molecular_functionNADP+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NDP A 2510
ChainResidue
AHIS54
APHE183
AASP184
ALEU185
AALA186
AARG309
AGLY312
AARG314
AARG315
APYC2520
AHOH2536
AHIS126
AHOH2545
AHOH2571
AHOH2576
AHOH2581
AHOH2634
AHOH2645
AHOH2709
AHOH2724
AHOH2728
AHOH2750
AALA128
BHIS157
BHIS236
BLYS237
BHOH1539
BHOH1640
AALA129
ALEU130
AVAL148
ASER150
ATHR166
APRO168

site_idAC2
Number of Residues33
DetailsBINDING SITE FOR RESIDUE NDP B 1510
ChainResidue
AHIS236
ALYS237
AHOH2533
AHOH2560
AHOH2697
BHIS54
BHIS126
BALA128
BALA129
BLEU130
BVAL148
BSER150
BTHR166
BPRO168
BPHE183
BASP184
BLEU185
BALA186
BARG309
BGLY312
BASP313
BARG314
BARG315
BPYC1520
BHOH1533
BHOH1580
BHOH1599
BHOH1611
BHOH1685
BHOH1741
BHOH1777
BHOH1779
BHOH1787

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYC A 2520
ChainResidue
AHIS54
AARG58
AMET151
ATHR166
AALA191
AHIS192
AGLY193
ANDP2510

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYC B 1520
ChainResidue
BHIS54
BARG58
BSER150
BMET151
BTHR166
BALA191
BHIS192
BGLY193
BNDP1510

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:16192274
ChainResidueDetails
ASER53
AASP194
BSER53
BASP194

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:16192274
ChainResidueDetails
AHIS54
BHIS54

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:16192274
ChainResidueDetails
AARG58
ATHR166
AHIS192
BARG58
BTHR166
BHIS192

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: in other chain => ECO:0000269|PubMed:16192274, ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH
ChainResidueDetails
AHIS126
AASP184
AARG309
BHIS126
BASP184
BARG309

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16192274, ECO:0007744|PDB:2CWF, ECO:0007744|PDB:2CWH
ChainResidueDetails
AHIS236
BHIS236

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
AHIS54

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
BHIS54

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PDB entries from 2024-07-17

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