Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1H0D

Crystal structure of Human Angiogenin in complex with Fab fragment of its monoclonal antibody mAb 26-2F

Functional Information from GO Data
ChainGOidnamespacecontents
C0001525biological_processangiogenesis
C0001541biological_processovarian follicle development
C0001556biological_processoocyte maturation
C0001666biological_processresponse to hypoxia
C0001890biological_processplacenta development
C0001938biological_processpositive regulation of endothelial cell proliferation
C0003676molecular_functionnucleic acid binding
C0003677molecular_functionDNA binding
C0003779molecular_functionactin binding
C0004519molecular_functionendonuclease activity
C0004521molecular_functionRNA endonuclease activity
C0004540molecular_functionRNA nuclease activity
C0005102molecular_functionsignaling receptor binding
C0005507molecular_functioncopper ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005604cellular_componentbasement membrane
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0005730cellular_componentnucleolus
C0005829cellular_componentcytosol
C0007154biological_processcell communication
C0008201molecular_functionheparin binding
C0009303biological_processrRNA transcription
C0009725biological_processresponse to hormone
C0015629cellular_componentactin cytoskeleton
C0016078biological_processtRNA decay
C0016477biological_processcell migration
C0017148biological_processnegative regulation of translation
C0019731biological_processantibacterial humoral response
C0019843molecular_functionrRNA binding
C0023052biological_processsignaling
C0030041biological_processactin filament polymerization
C0030154biological_processcell differentiation
C0030426cellular_componentgrowth cone
C0031410cellular_componentcytoplasmic vesicle
C0032311cellular_componentangiogenin-PRI complex
C0042277molecular_functionpeptide binding
C0042327biological_processpositive regulation of phosphorylation
C0042592biological_processhomeostatic process
C0042803molecular_functionprotein homodimerization activity
C0043025cellular_componentneuronal cell body
C0045087biological_processinnate immune response
C0048662biological_processnegative regulation of smooth muscle cell proliferation
C0050714biological_processpositive regulation of protein secretion
C0050830biological_processdefense response to Gram-positive bacterium
C0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1212
ChainResidue
ASER14
ALYS106
AHOH2130
CSER4
CARG5

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1216
ChainResidue
BHOH2034
BHOH2104
CARG21
BGLY53
BGLY54
BARG71
BILE73

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1124
ChainResidue
AHOH2101
CHIS13
CLYS40
CHOH2092
CHOH2093

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 1125
ChainResidue
CASN49
CLYS50
CARG51
CHOH2011

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 1126
ChainResidue
CHIS65
CARG66

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1127
ChainResidue
CTYR6
CLYS50
CLYS54

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 C 1128
ChainResidue
CARG32
CARG33

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1129
ChainResidue
CLYS60
CASN63
CHIS65

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1213
ChainResidue
ASER55
AARG208

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1214
ChainResidue
ASER64
AGLY65
ASER66
AHOH2055

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1215
ChainResidue
APRO8
AALA9
ASER10

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1216
ChainResidue
ATHR163
AASP164
AASP166
AHOH2110
AHOH2112
BHIS164

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1217
ChainResidue
AGLU122
BSER120
BVAL121
BTYR122
BSER202
BSER203
BLYS208
BHOH2098

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1218
ChainResidue
AGLN123
ASER126
BTYR122
BLYS143

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKdiNTF
ChainResidueDetails
CCYS39-PHE45

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
ATYR191-HIS197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11468363, ECO:0000269|PubMed:9918722
ChainResidueDetails
CHIS13

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11468363, ECO:0000269|PubMed:9918722
ChainResidueDetails
CHIS114

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
CLYS40

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:2866794
ChainResidueDetails
CPCA1

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4y
ChainResidueDetails
CHIS13
CLYS40
CHIS114

site_idMCSA1
Number of Residues3
DetailsM-CSA 564
ChainResidueDetails
CHIS13increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
CLYS40electrostatic stabiliser
CHIS114increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon