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1K1D

Crystal structure of D-hydantoinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
C0005737cellular_componentcytoplasm
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0046872molecular_functionmetal ion binding
D0005737cellular_componentcytoplasm
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0046872molecular_functionmetal ion binding
E0005737cellular_componentcytoplasm
E0016787molecular_functionhydrolase activity
E0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
E0046872molecular_functionmetal ion binding
F0005737cellular_componentcytoplasm
F0016787molecular_functionhydrolase activity
F0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
F0046872molecular_functionmetal ion binding
G0005737cellular_componentcytoplasm
G0016787molecular_functionhydrolase activity
G0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
G0046872molecular_functionmetal ion binding
H0005737cellular_componentcytoplasm
H0016787molecular_functionhydrolase activity
H0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AKCX150
AHIS183
AHIS239
AZN502

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AHIS58
AHIS60
AKCX150
AASP315
AZN501

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BKCX150
BHIS183
BHIS239
BZN502

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BHIS58
BHIS60
BKCX150
BASP315
BZN501

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 501
ChainResidue
CKCX150
CHIS183
CHIS239
CZN502

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 502
ChainResidue
CHIS58
CHIS60
CKCX150
CASP315
CZN501

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 501
ChainResidue
DKCX150
DHIS183
DHIS239
DZN502

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 502
ChainResidue
DHIS58
DHIS60
DKCX150
DASP315
DZN501

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 501
ChainResidue
EKCX150
EHIS183
EHIS239
EZN502

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 502
ChainResidue
EHIS58
EHIS60
EKCX150
EASP315
EZN501

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 501
ChainResidue
FKCX150
FHIS183
FHIS239
FZN502

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN F 502
ChainResidue
FHIS58
FHIS60
FKCX150
FASP315
FZN501

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 501
ChainResidue
GKCX150
GHIS183
GHIS239
GZN502

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN G 502
ChainResidue
GHIS58
GHIS60
GKCX150
GASP315
GZN501

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 501
ChainResidue
HKCX150
HHIS183
HHIS239
HZN502

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN H 502
ChainResidue
HHIS58
HHIS60
HKCX150
HASP315
HZN501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING: BINDING => ECO:0000269|PubMed:12135362, ECO:0007744|PDB:1K1D
ChainResidueDetails
AHIS58
BASP315
CHIS58
CHIS60
CHIS183
CHIS239
CASP315
DHIS58
DHIS60
DHIS183
DHIS239
AHIS60
DASP315
EHIS58
EHIS60
EHIS183
EHIS239
EASP315
FHIS58
FHIS60
FHIS183
FHIS239
AHIS183
FASP315
GHIS58
GHIS60
GHIS183
GHIS239
GASP315
HHIS58
HHIS60
HHIS183
HHIS239
AHIS239
HASP315
AASP315
BHIS58
BHIS60
BHIS183
BHIS239

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: via carbamate group => ECO:0000269|PubMed:12135362, ECO:0007744|PDB:1K1D
ChainResidueDetails
AKCX150
BKCX150
CKCX150
DKCX150
EKCX150
FKCX150
GKCX150
HKCX150

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9P903
ChainResidueDetails
ATYR155
DTYR155
DSER288
DASN337
ETYR155
ESER288
EASN337
FTYR155
FSER288
FASN337
GTYR155
ASER288
GSER288
GASN337
HTYR155
HSER288
HASN337
AASN337
BTYR155
BSER288
BASN337
CTYR155
CSER288
CASN337

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12135362
ChainResidueDetails
AKCX150
BKCX150
CKCX150
DKCX150
EKCX150
FKCX150
GKCX150
HKCX150

218853

PDB entries from 2024-04-24

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