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1U7H

Structure and a Proposed Mechanism for Ornithine Cyclodeaminase from Pseudomonas putida

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008473molecular_functionornithine cyclodeaminase activity
A0008652biological_processamino acid biosynthetic process
A0016829molecular_functionlyase activity
A0055129biological_processL-proline biosynthetic process
B0000166molecular_functionnucleotide binding
B0008473molecular_functionornithine cyclodeaminase activity
B0008652biological_processamino acid biosynthetic process
B0016829molecular_functionlyase activity
B0055129biological_processL-proline biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 911
ChainResidue
AALA224
AVAL225
AGLY227
ASER293
AHOH992
AHOH994

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 912
ChainResidue
BSER293
BHOH1104
BHOH1105
BALA224
BVAL225
BGLY227

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAD B 801
ChainResidue
ALYS331
AHOH1021
AHOH1143
BTHR84
BARG112
BTHR113
BGLY138
BALA139
BGLN140
BASP161
BTHR162
BVAL201
BTHR202
BALA203
BILE210
BVAL225
BGLY226
BASP228
BLYS232
BSER293
BVAL294
BGLY295
BHOH1080
BHOH1087
BHOH1096
BHOH1097
BHOH1101
BHOH1109
BHOH1143
BHOH1144

site_idAC4
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAD A 802
ChainResidue
ATHR84
AARG112
ATHR113
AGLY138
AALA139
AGLN140
AASP161
ATHR162
AVAL201
ATHR202
AALA203
AILE210
AVAL225
AGLY226
AASP228
ALYS232
ASER293
AVAL294
AGLY295
AHOH971
AHOH973
AHOH977
AHOH998
AHOH1002
AHOH1003
AHOH1004
AHOH1016
AHOH1018
AHOH1211
BLYS331

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 901
ChainResidue
AGLN38
AALA39
AALA61
AASP62
ALYS63

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 902
ChainResidue
AALA39
AHOH1149
AHOH1150
BLEU216
BPRO218
BSER286
BVAL288
BHOH992

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MPD B 903
ChainResidue
BSER64
BARG65
BALA92
BASP93
BVAL100
BLEU308
BHOH1254
BHOH1255
BHOH1256

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 904
ChainResidue
ATYR3
AALA311
AGLU312
AGLY315
AMSE316

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 905
ChainResidue
BTYR3
BALA311
BGLU312
BGLY315
BMSE316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15518536, ECO:0007744|PDB:1X7D
ChainResidueDetails
AASP228
BASP228

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15518536, ECO:0007744|PDB:1X7D
ChainResidueDetails
AARG45
ALYS69
AASP228
AVAL294
BARG45
BLYS69
BASP228
BVAL294

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:15518536, ECO:0007744|PDB:1U7H, ECO:0007744|PDB:1X7D
ChainResidueDetails
ATHR84
BTHR84
BARG112
BALA139
BASP161
BTHR202
BVAL225
BLYS232
BSER293
BLYS331
AARG112
AALA139
AASP161
ATHR202
AVAL225
ALYS232
ASER293
ALYS331

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 717
ChainResidueDetails
AGLU56increase nucleophilicity, proton acceptor, proton donor
AASP228proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 717
ChainResidueDetails
BGLU56increase nucleophilicity, proton acceptor, proton donor
BASP228proton acceptor, proton donor

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PDB entries from 2024-10-30

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