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4KXL

Crystal structure of DNPH1 (RCL) with 6-CYCLOPENTYL-AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0009159biological_processdeoxyribonucleoside monophosphate catabolic process
A0070694molecular_functiondeoxyribonucleoside 5'-monophosphate N-glycosidase activity
B0009159biological_processdeoxyribonucleoside monophosphate catabolic process
B0070694molecular_functiondeoxyribonucleoside 5'-monophosphate N-glycosidase activity
C0009159biological_processdeoxyribonucleoside monophosphate catabolic process
C0070694molecular_functiondeoxyribonucleoside 5'-monophosphate N-glycosidase activity
D0009159biological_processdeoxyribonucleoside monophosphate catabolic process
D0070694molecular_functiondeoxyribonucleoside 5'-monophosphate N-glycosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 6C6 A 201
ChainResidue
ACYS15
AILE65
AASN69
ASER87
AGLY89
AGLU93
AHOH304
AHOH305
AHOH322
BSER117
BMET119
AGLY16
ASER17
AILE18
AARG19
AGLY20
AHIS45
AVAL46
AGLU57

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 6C6 B 201
ChainResidue
ASER117
AMET119
BCYS15
BGLY16
BSER17
BILE18
BARG19
BGLY20
BILE65
BASN69
BSER87
BGLY89
BVAL90
BGLU93
BHOH304
BHOH322
BHOH359

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 6C6 C 201
ChainResidue
CCYS15
CGLY16
CSER17
CILE18
CARG19
CGLY20
CHIS45
CVAL46
CILE65
CASN69
CSER87
CGLY89
CGLU93
CHOH307
CHOH310
CHOH335
CHOH371
DSER117
DMET119

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 202
ChainResidue
CARG34
CARG37

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 6C6 D 201
ChainResidue
CSER117
CMET119
DCYS15
DGLY16
DSER17
DILE18
DARG19
DGLY20
DHIS45
DVAL46
DGLU57
DILE65
DASN69
DSER87
DGLY89
DGLU93
DHOH301
DHOH304
DHOH338
DHOH403

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 202
ChainResidue
DARG34
DARG37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:23385460, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359, ECO:0007744|PDB:4FYH, ECO:0007744|PDB:4FYI, ECO:0007744|PDB:4FYK, ECO:0007744|PDB:4KXL, ECO:0007744|PDB:4KXM, ECO:0007744|PDB:4KXN, ECO:0007744|PDB:4P5D
ChainResidueDetails
AGLY16
BARG19
BGLY20
BSER87
BGLY89
BGLU93
CGLY16
CILE18
CARG19
CGLY20
CSER87
AILE18
CGLY89
CGLU93
DGLY16
DILE18
DARG19
DGLY20
DSER87
DGLY89
DGLU93
AARG19
AGLY20
ASER87
AGLY89
AGLU93
BGLY16
BILE18

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: in other chain => ECO:0000269|PubMed:23385460, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359, ECO:0007744|PDB:4FYH, ECO:0007744|PDB:4FYI, ECO:0007744|PDB:4FYK, ECO:0007744|PDB:4KXL, ECO:0007744|PDB:4KXM, ECO:0007744|PDB:4KXN, ECO:0007744|PDB:4P5D
ChainResidueDetails
ASER117
BSER117
CSER117
DSER117

site_idSWS_FT_FI3
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O43598
ChainResidueDetails
ASER17
CSER87
CSER112
CSER127
DSER17
DSER87
DSER112
DSER127
ASER87
ASER112
ASER127
BSER17
BSER87
BSER112
BSER127
CSER17

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER117
BSER117
CSER117
DSER117

222036

PDB entries from 2024-07-03

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